Online Table 1. Data on transcription-factor interactions in Escherichia coli (html version)

Wall, M. E., Hlavacek, W. S. & Savageau, M. A. Design of gene circuits: lessons from bacteria. Nat. Rev. Genet. 5, 34-42 (2004)

Download a reprint (pdf) of Wall ME et al. (2004)

Download the pdf version of supplementary Online Table 1.

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    Caption (provides an overview of the table)
    Table sections: (each section corresponds to a distinct type of gene circuit)
      ACTIVATOR control of INDUCIBLE effector gene expression
      REPRESSOR control of INDUCIBLE effector gene expression
      ACTIVATOR control of REPRESSIBLE effector gene expression
      REPRESSOR control of REPRESSIBLE effector gene expression
    Notes (additional information, mostly via links, about each TF and an alphabetical list of the TFs)
    Resources (description of the types of links in the Notes section and other information about further resources)
    Legal Notices (conditions of use, policy and disclaimers, privacy notice, copyright notice, etc.)
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Caption (top)

This table summarizes information about autoregulation of 50 transcription factors (TFs) in E. coli (e.g., the TF LacI, the repressor of the lac operon) and the signals (e.g., allolactose, the small molecule that binds LacI, inhibiting the repressor's ability to bind DNA) that influence how the TFs affect transcription. The table and our motivation for compiling it are discussed in a Nature Reviews Genetics paper (Wall ME et al., 2004) [PubMed abstract | html | pdf]. The first 34 systems included in the table are inducible (i.e., effector gene expression increases with an increase in signal), and the following 16 are repressible (i.e., effector gene expression decreases with an increase in signal). Within each of these two classes, systems with activator-controlled effector genes are listed first, and then systems with repressor-controlled effector genes are listed. An effector gene is a gene that encodes, for example, a catabolic or biosynthetic enzyme, membrane transporter, flagellar protein, etc. The signal molecule in an inducible system is called an inducer (Ind). For some inducible systems, an anti-inducer (AntiInd) can competitively bind at the inducer binding site, inhibiting induction. The signal molecule in a repressible system is called a co-repressor (CoR). The term "de-activator" is sometimes used in the literature as an alternative name for the signal when repressible effector genes are under the control of an activator. A TF can act as a repressor or an activator at the promoter(s) of a transcriptional unit (TU). A TU consists of a single gene or an operon. A regulator TU encodes a TF, and an effector TU encodes one or more effector genes. A TU can be both a regulator and effector TU if a TF gene is co-transcribed with effector genes. Next to each regulator TU listed in the table there appears in parentheses a symbol that indicates the mode ofautoregulation: &minus, negative autoregulation of the regulator TU by the encoded TF; +, positive autoregulation of the regulator TU by the encoded TF; or 0, no autoregulation. Likewise, the mode of TF activity at the promoter(s) of each effector TU is indicated. The term "dual" indicates that the TF has both repressor and activator activity at the promoter(s) of a TU. The form of coupling (I, U or D) indicates how regulator and effector TUs are co-regulated in response to a change in signal: "I" indicates inverse coupling (opposite changes in regulator and effector expression with a change in signal), "U" indicates uncoupling (no change in regulator gene expression with changes in effector gene expression), and "D" indicates direct coupling (coordinate changes in regulator and effector gene expression). Each signal molecule is labeled as an inducer of effector gene expression (Ind), an anti-inducer (AntiInd) of effector gene expression, or a co-repressor/de-activator or effector gene expression (CoR). In some cases, the signal is not a molecule but a modification of the TF (e.g., phosphorylation). Also, in some cases, the signal acts as an inducer of some genes but as a co-repressor of other genes. Note that the influence of the signal on transcription (Ind or CoR) is indicated only for effector genes; the influence of the signal on regulator gene expression can be inferred from the form of coupling. Question marks indicate uncertainty or gaps in our knowledge. The references provided for each entry were selected for one or more of the following reasons: a paper reports the influence of the TF on expression of its own gene, a paper reports the influence of the signal on expression of the regulator TU, and/or a paper identifies a signal that affects the activity of the TF. In some cases, a paper is cited because it reports how a TF or signal influences one or more effector TUs, but we have not tried to provide a comprehensive bibliography of such papers. In the case of a (global) TF that regulates a large number of genes, we have not attempted to provide a comprehensive list of regulated effector TUs. RegulonDB Uri Alon's web site, and EcoCyc each provide information about effector TUs that are not listed here for some TFs. Notes are provided below the table; there is a note for every table entry. Click on the name of a TF (e.g., AraC) to see the note for that entry. Each note provides links to various online resources where additional information about each TF can be found; the links are TF specific. Note that there are legal notices at the bottom of this page. Please send email to ecotfs@lanl.gov if you have questions or feedback for us.


ACTIVATOR CONTROL OF INDUCIBLE EFFECTOR GENE EXPRESSION (top)
TF Regulator TU(s) Efffector TU(s) Coupling Signal(s) Reference(s)
AraC araC (&minus) araBAD (dual +/&minus)
araE (+)
araFGH (+)
araJ (+)
I (see note) L-arabinose (Ind)
D-fucose (AntiInd)
Doyle ME et al. (1972)
Casadaban MJ (1976)
Hahn S & Schleif R (1983)
Schlief R (1987)
Johnson CM & Schleif RF (1995)
Schleif R (2000)
Schleif R (2003)
CpxR cpxRA (+) cpxP (+)
degP (+)
ppiA (+)
rdoA-dsbA (+)
csgBA (&minus)
csgDEFG (&minus)
many others (+, &minus)
D phosphorylation of CpxR (Ind) Pogliano J et al. (1997)
De Wulf P et al. (1999)
Raivio TL et al. (1999)
Prigent-Combaret C et al. (2001)
De Wulf P et al. (2002)
CynR cynR (&minus) cynTSX (+) U cyanate (Ind) Sung YC & Fuchs JA (1992)
Guilloton MB et al. (1993)
Lamblin AFJ & Fuchs JA (1994)
CysB cysB (&minus) cysJIH (+)
cysK (+)
cysPTWA(M?) (+)
others (+, &minus)
D N-acetyl-L-serine (Ind)
sulfide (AntiInd)
thiosulfate (AntiInd)
Jagura-Burdzy G & Hulanicka D (1981)
Ostrowski J & Kredich NM (1991)
Hryniewicz MM & Kredich NM (1991)
Kredich NM (1992)
Lynch AS et al. (1994)
Kredich NM (1996)
DsdC dsdC (&minus) dsdXA (+) D D-serine (Ind) Heincz MC & McFall E (1978)
McFall E & Heincz MC (1983)
Heincz MC et al. (1984)
Norregaard-Madsen M et al. (1995)
IdnR idnDOTR (+) idnDOTR (+)
idnK (+)
gntKU (&minus)
gntT (&minus)
D (for idn genes, I for gnt genes) L-idonate (Ind for idn genes, CoR for gnt genes) Bausch C et al. (1998)
Peekhaus N & Conway T (1998)
Tsunedomi R et al. (2003a)
IlvY ilvY (&minus) ilvC (+) I (see note) &alpha-acetolactate (Ind)
&alpha-acetohydroxybutyrate (Ind)
Arfin SM et al. (1969)
Wek RC & Hatfield GW (1988)
Rhee KY et al. (1998)
MalT malT (0) malEFG (+)
malK-lamB-malM (+)
malPQ (+)
malS (+)
malZ (+)
U (see note) ATP + maltotriose (Ind)
Aes (AntiInd)
MalK (CoR)
MalY (AntiInd)
Debarbouille M & Schwartz M (1979)
Raibaud O & Richet E (1987)
Richet E & Raibaud O (1989)
Raibaud O et al. (1991)
Panagiotidis CH et al. (1998)
Boos W & Shuman H (1998)
Schreiber V et al. (2000)
Joly N et al. (2002)
MarA marRAB (+) acrAB (+)
micF (+)
many others (+)
D none
see MarR entry
Martin RG et al. (1996) Martin RG & Rosner JL (2002)
Barbosa TM & Levy SB (2002)
MelR melR (&minus) melAB (+) D melibiose (Ind) Webster C et al. (1989)
Belyaeva TA et al. (2000)
Wade JT et al. (2000)
MetR metR (&minus) glyA (+/&minus)
metA (+)
metE (+)
metF (+)
metH (+)
I homocysteine (Ind, CoR of metA and metH) Urbanowski ML & Stauffer GV (1987)
Maxon ME et al. (1989)
Cai XY et al. (1989)
Urbanowski ML & Stauffer GV (1989a)
Urbanowski ML & Stauffer GV (1989b)
Mares R et al. (1992)
Cowan JM et al. (1993)
Lorenz E & Stauffer GV (1996)
MhpR mhpR (0) mhpABCDEF-mhpT (+) U 3-(3-hyroxyphenyl)propionic acid (Ind) Ferrandez et al. (1997)
Torres B et al. (2003)
RhaR rhaSR (+) rhaSR (+)
see RhaS entry
D L-rhamnose (Ind)
L-lyxose (Ind)
L-mannose (Ind)
Tobin JF & Schleif RF (1987)
Tobin JF & Schleif RF (1990a)
Tobin JF & Schleif RF (1990b)
Badia J et al. (1991)
Egan SM & Schleif RF (1993)
Via P et al. (1996)
RhaS rhaSR (&minus) rhaBAD (+)
rhaT (+)
D L-rhamnose (Ind)
L-lyxose (Ind)
L-mannose (Ind)
Egan SM & Schleif RF (1993)
Via P et al. (1996)
Rob rob (0) acrAB (+)
inaA (+)
galT (&minus)
others (+)
U dipyridyl (Ind)
decanoate (Ind)
Bennik MH et al. (2000)
Rosner JL et al. (2002)
Rosenberg EY et al. (2003)
SoxR soxR (&minus) soxS (+) U oxidation of SoxR-bound [2Fe-2S] (Ind) Hidalgo E et al. (1995)
Hidalgo E et al. (1998)
SoxS soxS (&minus) sodA (+)
many others (+)
I none
see SoxR entry
Nunoshiba T et al. (1993)
Griffith KL & Wolf RE Jr (2002)
TorR torR (&minus) torCAD (+)
others (+, &minus)
U phosphorylation of TorR (Ind) Simon G et al. (1995)
Ansaldi M et al. (2000)
Bordi C et al. (2003)
XapR xapR (0) xapAB (+) U xanthosine (Ind) Seeger C et al. (1995)
Jorgensen C & Dandanell G (1999)
XylR xylFGHR (+)
xylR (0)
xylAB (+)
xylFGHR (+)
D D-xylose (Ind) Song S & Park C (1997)
Gonzalez R et al. (2002)
REPRESSOR CONTROL OF INDUCIBLE EFFECTOR GENE EXPRESSION (top)
TF Regulator TU(s) Efffector TU(s) Coupling Signal(s) Reference(s)
BetI betIBA (&minus) betIBA (&minus)
betT (&minus)
D choline (Ind) Lamark T et al. (1996)
Rokenes TP et al. (1996)
CytR
(and cAMP-CRP)
cytR (&minus) cdd (&minus)
deoCABD (&minus)
nupC (&minus)
nupG (&minus)
ppiA (&minus)
rpoH (&minus)
tsx (+/&minus)
udp (&minus)
D cytidine (Ind) Gerlach P et al. (1990)
Pedersen H et al. (1992)
Valentin-Hansen P et al. (1996)
EmrR emrRAB (&minus) emrRAB (&minus) D 2,4-dinitrophenol (Ind)
others (Ind)
Lomovskaya O et al. (1995)
Brooun A et al. (1999)
Xiong A et al. (2000)
GalR galR (0) galETKM (&minus)
galP (&minus)
galS (&minus)
U &beta-D-galactose (Ind)
D-fucose (Ind)
Buttin G (1963)
Weickert MJ & Adhya S (1993a)
Weickert MJ & Adhya S (1993b)
Brown MP et al. (1994)
GalS galS (&minus) mglBAC (&minus)
galETKM (&minus)
D &beta-D-galactose (Ind)
D-fucose (Ind)
Weickert MJ & Adhya S (1992)
Weickert MJ & Adhya S (1993a)
Weickert MJ & Adhya S (1993b)
Geanacopoulos M & Adhya S (1997)
GlpR glpEGR (0)
glpGR (0)
glpR (0)
glpACB (&minus)
glpD (&minus)
glpFKX (&minus)
glpTQ (&minus)
U sn-glycerol 3-phosphate (Ind)
D-galactose 1-phosphate (AntiInd)
Sundararajan TA (1963)
Hayashi SI & Lin EC (1965)
Lin EC (1976)
Larson TJ et al. (1987)
Zeng G et al. (1996)
Yang B & Larson TJ (1998)
LacI lacI (0) lacZYA (&minus) U allolactose (Ind)
IPTG (Ind)
Novick A et al. (1965)
Gilbert W & Muller-Hill B (1966) PNAS 56:1891-8.
Muller-Hill B & Kania J (1974)
MarR marRAB (&minus) marRAB (&minus) D salicylate (Ind)
other phenolic compounds (Ind)
Cohen SP et al. (1993a)
Cohen SP et al. (1993b)
Ariza RR et al. (1994)
Seoane AS & Levy SB (1995)
NagC nagBACD (&minus)
nagC (0)
glmUS (+/&minus)
manXYZ (&minus)
nagBACD (&minus)
nagE (&minus)
D N-acetylglucosamine 6-phosphate (Ind) Plumbridge JA (1991)
Plumbridge J (1996)
PdhR pdhR-aceEF-lpdA (&minus) pdhR-aceEF-lpdA (&minus) D pyruvate (Ind) Quail MA et al. (1994)
Quail MA & Guest JR (1995)
PutA putA (&minus) putA (&minus)
putP (&minus)
D proline (Ind) Brown ED & Wood JM (1992)
RbsR rbsDACBK(R?) (&minus)
rbsKR? (0)
rbsDACBK(R?) (&minus) U? D-ribose (Ind) Lopilato JE et al. (1984)
Mauzy CA & Hermodson MA (1992a)
TreR treR (?)
treBC (&minus) ? trehalose 6-phosphate (Ind)
trehalose (AntiInd)
Horlacher R & Boos W (1997)
Hars U et al. (1998)
UxuR
(and ExuR)
uxuR (&minus) uxuAB (&minus) D D-fructuronate (Ind) Ritzenthaler P & Mata-Gilsinger M (1982)
Hugouvieux-Cotte-Pattat N & Robert-Baudouy J (1983)
Ritzenthaler P & Mata-Gilsinger M (1983)
Ritzenthaler P et al. (1985)
Rodionov DA et al. (2000)
ACTIVATOR CONTROL OF REPRESSIBLE EFFECTOR GENE EXPRESSION (top)
TF Regulator TU(s) Efffector TU(s) Coupling Signal(s) Reference(s)
AsnC asnC (&minus) asnA (+) U asparagine (CoR) Kolling R & Lother H (1985)
de Wind N et al. (1985)
Poggio S et al. (2002)
FadR fadR (0) fabA (+)
fabB (+)
iclR (+)
fadBA (&minus)
fadD (&minus)
fadE (&minus)
fadIJ (&minus)
fadL (&minus)
uspA (&minus)
U long-chain acyl-CoA (CoR of positively regulated genes, Ind of negatively regulated genes) Henry MF & Cronan JE Jr (1992)
Raman N & DiRusso CC (1995)
Gui L et al. (1996b)
Farewell A et al. (1996)
Campbell JW & Cronan JE Jr (2001)
Campbell JW & Cronan JE Jr (2002)
Campbell JW et al. (2003)
FruR (also called Cra) fruR (0) aceBAK (+)
icd (+)
pckA (+)
ppsA (+)
adhE (&minus)
edd-eda (&minus)
fruBKA (&minus)
gapB-pgk (&minus)
mtlADR (&minus)
nirBDC-cysG (&minus)
pfkA (&minus)
pykF (&minus)
ptsHI-crr (dual &minus/+)
U D-fructose-1-phosphate (CoR of positively regulated genes, Ind of negatively regulated genes)
fructose-1,6-bisphosphate (same as above)
Chin AM et al. (1989)
Ramseier TM et al. (1993)
Ramseier TM et al. (1995)
Saier MH Jr & Ramseier TM (1996)
GcvA gcvA (&minus) gcvTHP (dual +/&minus) U glycine-free GcvR (CoR)
The system is glycine inducible.
Wilson RL et al. (1993a)
Wilson RL et al. (1993b)
Wilson RL & Stauffer GV (1994)
Wilson RL et al. (1995)
Ghrist AC & Stauffer GV (1998)
Wonderling LD et al. (2000)
Heil G et al. (2002)
PspF pspF (&minus) pspABCDE (+) U PspA (CoR) Jovanovic G et al. (1997)
Elderkin S et al. (2002)
REPRESSOR CONTROL OF REPRESSIBLE EFFECTOR GENE EXPRESSION (top)
TF Regulator TU(s) Efffector TU(s) Coupling Signal(s) Reference(s)
ArgR argR (&minus) argCBH (&minus)
argD (&minus)
argE (&minus)
argF (&minus)
argI (&minus)
carAB (&minus)
possibly others
D L-arginine (CoR) Cunin R et al. (1976)
Lim DB et al. (1987)
Tian G et al. (1994)
Maas WK (1994)
DnaA dnaA (&minus) dnaA (&minus)
others (&minus, +)
D ATP (CoR) Messer W & Weigel C (1997)
Speck C et al. (1999)
Fur fldA-fur (?)
fur (&minus)
iron transport genes and others (&minus, +) D Fe2+ (CoR) de Lorenzo V et al. (1988)
Escolar L et al. (1999)
Zheng M et al. (1999)
Hantke K (2001)
Andrews SC et al. (2003)
McHugh JP et al. (2003)
H-NS hns (&minus) hns (&minus)
others (&minus, +)
D DNA curvature (CoR) Atlung T & Ingmer H (1997)
Schroder O & Wagner R (2002)
IscR iscRSUA (&minus) iscRSUA (&minus) D [2Fe-2S] (CoR) Schwartz CJ et al. (2001)
MazEF mazEF (&minus)
relA-mazEF (0)
mazEF (&minus) D guanosine-3',5'-bispyrophosphate (CoR) Aizenman E et al. (1996)
Marianovsky I et al. (2001)
MetJ metJ (&minus) metA (&minus)
metBL (&minus)
metC (&minus)
metE (&minus)
metF (&minus)
metNIQ (&minus)
metR (&minus)
others likely
D S-adenosyl-L-methionine (CoR) Saint-Girons I et al. (1984)
Shoeman R et al. (1985)
Urbanowski ML & Stauffer GV (1986)
Weissbach H & Brot N (1991)
Old IG et al. (1991)
ModE modEF (0) dmsABC (&minus)
modABCD (&minus)
moaABCDE (+)
others (see note)
U molybdate (CoR of dmsABC and modABCE, Ind of moaABCDE)
tungstate (same as above)
Grunden AM et al. (1996)
McNicholas PM et al. (1998)
Anderson LA et al. (2000)
PurR purR (&minus) cvpA-purF-dedF (&minus)
guaBA (&minus)
purA (&minus)
purB (&minus)
purC (&minus)
purER (&minus)
purHD (&minus)
purL (&minus)
purMN (&minus)
purT (&minus)
others (&minus)
D hypoxanthine (CoR)
guanine (CoR)
and analogues
Meng LM et al. (1990a)
Meng LM & Nygaard P (1990b)
Rolfes RJ & Zalkin H (1990a)
Rolfes RJ & Zalkin H (1990b)
Choi KY & Zalkin H (1992)
Zalkin H & Nygaard P (1996)
TrpR trpR (&minus) aroH (&minus)
aroL (&minus)
mtr (&minus)
trpLEDCBA (&minus)
D L-tryptophan (CoR) Klig LS et al. (1988)
Somerville R (1992)
TyrR tyrR (&minus) aroF-tyrA (&minus)
aroL (&minus)
aroP (&minus)
mtr (+)
tyrB (&minus)
tyrP (&minus)
others (see note)
U ATP + L-tyrosine (CoR, Ind of mtr)
others (see note)
Camakaris H & Pittard J (1982)
Pittard AJ & Davidson BE (1991)

Notes ordered alphabetically by TF name (top)

  1. AraC [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): HTH_AraC (2x), AraC_binding
    AraC is a member of the AraC/XylS family. During induction, araC is transiently induced. Expression then falls below the background level. See Johnson CM & Schleif RF (1995). Also see earlier reports (Ogden S et al., 1980; Hahn S & Schleif R, 1983; Stoner CM & Schleif RF, 1983). In the absence of arabinose, AraC represses expression of araBAD, whereas in the presence of arabinose, AraC activates expression of araBAD. The promoters of araE and araJ are similar to that of araBAD; the promoter of araFGH is different.

  2. ArgR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): Arg_repressor, Arg_repressor_C
    ArgR is a member of the ArgR family. Expression of argA is regulated by L-arginine (Leisinger T & Haas D, 1975), and argG also seems to be part of the arginine regulon (Glansdorff, 1987).

  3. AsnC [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): AsnC_trans_reg
    AsnC is a member of the AsnC/Lrp family.

  4. BetI [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): TetR_N
    BetI is a member of the TetR/AcrR family of TFs.

  5. CpxR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): Response_reg, Trans_reg_C

  6. CynR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): HTH_1, LysR_substrate
    CynR is a member of the LysR family.

  7. CysB [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): HTH_1, LysR_substrate
    CysB is a member of the LysR family; it contains multiple domains (Lochowska A et al., 2001). cysU=cysT. Autoregulation of cysB is not responsive to sulfide or sulfur source (Jagura-Burdzy G & Hulanicka D, 1981; Ostrowski J & Kredich NM, 1991) but is responsive to acetylserine (Ostrowski J & Kredich NM, 1991; Hryniewicz MM & Kredich NM, 1991). Other effector TUs regulated by CysB include cbl or nac-cbl (+, Iwanicka-Nowicka R & Hryniewicz MM, 1995), cysDNC (+), possibly hslJ (&minus, Lilic M et al., 2003), ssuEADCB (&minus, Bykowski T et al., 2002) and tauABCD (+, van der Ploeg JR et al., 1997).

  8. CytR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): LacI, Peripla_BP_1
    CytR is a member of the GalR/LacI family of TFs. The nucleoprotein complex of CytR and DNA-bound cAMP-CRP negatively regulates the following promoters: deoP2, udpP, nupG-P, cddP, tsx-P2, cytXp-rotP2-P4, and rpoH-P3-P4-P5 (Valentin-Hansen et al., 1996; Kallipolitis & Valentin-Hansen, 1998). The inducer, cytidine, does not affect CytR-DNA interaction but interferes with protein-protein interactions of CytR and CRP.

  9. DnaA [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): Bac_DnaA
    DnaA is a bacterial dnaA protein.

  10. DsdC [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): HTH_1, LysR_substrate
    DsdC is a member of the LysR family.

  11. EmrR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): MarR
    EmrR is a member of the MarR family. Abbreviation: DNP, 2,4-dinitrophenol. EmrR is also called MprA.

  12. FadR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): GntR
    FadR is a member of the GntR family; it is homologous to the regulatory domains of TetR family members. Note that yfcYX has been renamed fadIJ. fadE=yafH.

  13. FruR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): LacI, Peripla_BP_1
    FruR is a member of the LacI family. Expression of fruR appears to be regulated directly or indirectly by FruR (there is two-fold higher expression of fruR-lacZ in a fruR&minus background); however, in vitro studies indicate that FruR does not bind near the fruR regulatory region in the presence or absence of effector. Of the two effectors, fructose 1-phosphate seems to bind FruR more tightly. Note that gapB is also called epd.

  14. Fur [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): FUR
    Fur is a member of the Fur family. The mechanism of Fe2+-Fur activation appears to be indirect in some cases. rhyB, which is repressed by Fe2+-Fur, specifies a small non-coding RNA that negatively regulates genes that are activated (indirectly) by Fe2+-Fur. Fur acts as a repressor in most cases.

  15. GalR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): LacI, Peripla_BP_1
    GalR is a member of the LacI/GalR family. GalR regulates galP, galETKM (the gal operon), and mglBAC.

  16. GalS [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): LacI, Peripla_BP_1
    GalS is a member of the LacI/GalR family. GalS and GalR bind the same operators but the order of affinities is reversed. For example, GalS (GalR) binds the operator of mglBAC most (least) tightly.

  17. GcvA [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): HTH_1, LysR_substrate
    GcvA is a LysR-type transcriptional regulator. The gcvTHP operon is induced by glycine and repressed by purines (e.g., inosine). Glycine-free GcvR binds GcvA. The complex of GcvR and GcvA represses transcription of the gcvTHP operon. The interaction between GcvR and GcvA is disrupted when glycine binds GcvR. GcvR-free GcvA activates transcription of the gcvTHP operon. Expression of GcvR is constitutive, i.e., GcvR expression is not affected by GcvA, by GcvR, or by changes in the level of glycine. Similarly, expression of GcvA is unaffected by changes in the level of glycine, but in contrast mechanistically, GcvA is negatively autoregulated.

  18. GcvR directly interacts with glycine and, in the absence of glycine, with GcvA. Glycine-free GcvR forms a complex with GcvA that represses transcription of gcvTHP. GcvR-free GcvA activates transcription of gcvTHP. Expression of GcvR is constitutive, i.e., GcvR expression is not affected by GcvA, by GcvR, or by changes in the level of glycine. Note that GcvR is similar to PspA, in that each is protein that acts as a co-repressor to modulate the activity of a transcription factor. Interestingly, expression of PspA, which modulates the activity of PspF, is regulated by PspF, whereas expression of GcvR is not regulated by GcvA.

  19. GlpR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): DeoR
    GlpR is a member of the DeoR family. There is some confusion about the order/nomenclature of the glpA operon: it is glpABC or glpACB.

  20. H-NS [ Table Entry | EcoCyc | EcoGene | coliBASE ]
    Pfam domain(s): Histone_HNS
    H-NS is a histone-like nucleoid-structuring protein.

  21. IdnR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): LacI, Peripla_BP_1
    IdnR is also called GntH. The inducer is believed to be L-idonate but 5-ketogluconate cannot be ruled out. idnR is expressed from the promoter of the idnDOTR operon and also from its own constitutive promoter. The idnDOTR operon is also called the idnDO-gntWH operon.

  22. IlvY [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): HTH_1, LysR_substrate
    IlvY is a member of the LysR family. Wek & Hatfield (1988) observed a small decrease (a less than two-fold change) in expression of ilvY in the presence of inducer. See Rhee et al. (1999), Opel & Hatfield (2001), and Opel et al. (2001).

  23. IscR [ Table Entry | EcoCyc | EcoGene | coliBASE ]
    Pfam domain(s): Rrf2
    IscR contains an Fe-S cluster, [2Fe-2s]. This cluster is required for repressor activity. When cluster assembly is blocked, expression of the isc operon is elevated. Expression of the isc operon is also elevated in the presence of hydrogen peroxide (Zheng M et al., 2001).

  24. LacI [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): LacI, Peripla_BP_1
    LacI is a member of the LacI/GalR family.

  25. MalT [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): GerE
    MalT is a member of the MalT or LAL family (and the LuxR/UhpA family) and consists of four domains (Danot O, 2001): DT1, DT2, DT3, and DT4. MalT is inactive in monomeric form; it is active in oligomeric form. Maltotriose promotes oligomerization of MalT; activation requires that MalT bind not only maltotriose but also ATP. The proteins MalY and Aes compete with maltotriose for binding to MalT and stablize MalT in the monomeric form. MalY and Aes bind to the same portion (DT1 to DT2) of MalT (Schlegel A et al., 2002). MalK binds to a different part of MalT (perhaps DT3). MalK is a membrane protein. It inhibits MalT activity through sequestration of MalT. Although malT expression is not autoregulated by MalT, malT expression does decrease slightly (up to a 2-fold change) in the presence of the inducer (because of cAMP-CRP).

  26. MarA [ Table Entry | EcoCyc | EcoGene | coliBASE ]
    Pfam domain(s): HTH_AraC (2x)
    MarA is a member of the AraC/XylS family. MarA consists of two HTH domains linked by a long &alpha-helix (Rhee S et al., 1998). Martin RG et al. (2002) propose a mechanism for MarA activation that depends on MarA-RNAP complex formation. Consistent with the structure of MarA (just two HTH domains), no small-molecule ligand is known to interact with MarA.

  27. MarR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): MarR
    MarR is a member of the MarR family.

  28. MazEF [ Table Entry | EcoCyc], MazE [ EcoCyc | EcoGene | coliBASE ], MazF [ EcoCyc | EcoGene | coliBASE ]
    Pfam domain(s): SpoVT_AbrB in MazE, PemK in MazF
    Abbreviation: ppGpp, guanosine-3'-5'-bispyrophosphate. MazE represses mazEF transcription in the absence of MazF, but the complex of MazE and MazF is a more efficient repressor. MazE is also called ChpR, and MazF is also called ChpA.

  29. MelR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): HTH_AraC (2x)
    MelR is a member of the AraC family?

  30. MetJ [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): MetJ
    MetJ is a member of the MetJ family. MetJ contains a ribbon-helix-helix DNA-binding motif. metJ and metBL are adjacent. Likewise, metE and metR are adjacent. A number of MetJ binding siteshave been predicted (Liu R et al., 2001).

  31. MetR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): HTH_1, LysR_substrate
    MetR is a member of the LysR family. MetR also regulates hmp in a homocysteine-dependent manner (Membrillo-Hernandez J et al., 1998).

  32. MhpR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): IclR
    MhpR is a member of the IclR family. It is unclear whether transcription starting from the mhpA promoter continues through to mhpT or not. Abbreviation: 3HPP, 3-(3-hydroxyphenyl)propionic acid.

  33. ModE [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): HTH_9, TOBE (2x)
    ModE has a known three-dimensional structure (Hall DR et al., 1999). Molybdate (MoO42-) binding changes the conformation of ModE (Gourley DG et al., 2001). ModE binds molybdate and tungstate, an analogue of molybdate, indistinguishably (Anderson LA et al., 1997; Gourley DG et al., 2001; Anderson LA et al., 2000). Molybdate-bound ModE is a secondary transcriptional activator of hycABCDEFGH and narXL (Self WT et al., 1999). Molybdate-bound ModE is required for full expression of napFDAGHBC under certain conditions (McNicholas PM & Gunsalus P, 2002).

  34. NagC [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): ROK
    NagC is a member of the NagC/XylR family. Abbreviation: GlcNAc-6-P, N-acetylglucosamine-6-phosphate. NagC has dual activator/repressor effects on transcription of glmUS (Plumbridge J, 1995)

  35. PdhR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): GntR
    PdhR is a member of the GntR family. pdhR=genA

  36. PspF [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): Sigma54_activat

  37. PurR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): LacI, Peripla_BP_1
    PurR is a member of the LacI/GalR family. PurR is the only known regulator of the TUs listed in the table with the exceptions of guaBA and purA (Zalkin H & Nygaard P, 1996). (DnaA affects expression of guaBA.) These ten effector TUs are required for synthesis of AMP and GMP. PurR also regulates pyrC, pyrD, codBA, prs, glyA, the gcv operon, speA, and glnB. As a rule, these TUs are regulated not only by PurR but also by one or more additional TFs. dedF may not actually be part of the cvpA-purF-dedF operon. The toxic purine analogues 6-mercaptopurine and 6-thioguanine are also co-repressors. The two natural co-repressors bind PurR cooperatively.

  38. PutA [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): Pro_dh, Aldedh

  39. RbsR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): LacI, Peripla_BP_1
    RbsR is a member of the LacI family (Mauzy CA & Hermodson MA, 1992b). It is not entirely clear that rbsR is part of the rbs operon (Lopilato JE et al., 1984; Mauzy CA & Hermodson MA, 1992a). Lopilato JE et al. (1984) suggested that rbsR is part of a separate TU, i.e., not transcribed with the rest of the rbs genes. However, Mauzy CA & Hermodson MA (1992a) detected a transcript longer than expected based on the transcription terminators located within/near the rbsR gene, which suggests that rbsK and rbsR are co-transcribed. It is possible that rbsKR is expressed from a promoter upstream of rbsK or rbsDACBKR may constitute an operon, with down regulation of rbsR due to the transcription terminators located in/near this gene. Thus, the form of coupling is U or D.

  40. RhaR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): AraC_binding, HTH_AraC (2x)
    RhaR is a member of the AraC/XylS family.

  41. RhaS [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): AraC_binding, HTH_AraC (2x)
    RhaS is a member of the AraC/XylS family.

  42. Rob [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): HTH_AraC (2x), AraC_E_bind
    Rob is a member of the AraC/XylS family. Rob is part of the MarA/Rob/SoxS regulon. These three TFs regulate many of the same genes.

  43. SoxR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): MerR
    SoxR is a member of the MerR family.

  44. SoxS [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): HTH_AraC (2x)
    SoxS is a member of the AraC/XylS family. SoxS is part of the MarA/Rob/SoxS regulon. These three TFs regulate many of the same genes.

  45. TorR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): Response_reg, Trans_reg_C
    Two-component system. TorS is the sensor; it detects trimethylamine N-oxide (TMAO).

  46. TreR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): LacI, Peripla_BP_1
    TreR is a member of the LacI/GalR family. Autoregulation of treR has not been studied.

  47. TrpR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): Trp_repressor
    TrpR is a member of the TrpR family. It was reported that WrbA associates with TrpR and affects TrpR binding to DNA (Yang W et al., 1993), but in a later study, this effect of WrbA on TrpR was found to be non-specific (Grandori R et al., 1998). The aroL and mtr operons are regulated by both TrpR and TyrR. aroL is expressed as short and long transcripts; the long transcript is polycistronic: aroL-yaiA-aroM.

  48. TyrR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): ACT, Sigma54_activat, HTH_8
    TyrR is a member of the EBP family. TyrR contains a CTD Cro-like HTH DNA-binding motif. TyrR contains two other Pfam domain(s): The NTD domain binds RNAP, and the central domain binds ATP. TyrR, which is related to NtrC, has ATPase activity. The primary signal recognized by TyrR is L-tyrosine, but L-phenylalanine and L-tryptophan also affect the activity of TyrR. Phe acts as a co-repressor for TyrR repression of aroF-tyrA, aroG, and aroP. Trp acts as a co-repressor for TyrR repression of aroG and aroP. TyrR represses tyrP when bound to Tyr (CoR), as indicated in the table, but activates tyrP when bound to Phe (Ind). Tyr and Phe act as inducers of mtr expression, which is positively regulated by TyrR. TyrR and TrpR may interact to effect control of aroL and mtr. aroH may be regulated by TyrR. aroL is expressed as short and long transcripts; the long transcript is polycistronic: aroL-yaiA-aroM.

  49. UxuR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): GntR
    UxuR cooperates with ExuR (the two TFs form hetero-oligomers) to repress expression of uxuR and uxuAB (Ritzenthaler P & Mata-Gilsinger M, 1983; Ritzenthaler P et al., 1985).

  50. XapR [ Table Entry | EcoCyc | EcoGene | coliBASE | PDB BLAST (NCBI) ]
    Pfam domain(s): HTH_1, LysR_substrate
    XapR is a member of the LysR family.

  51. XylR [ Table Entry | EcoCyc | EcoGene | coliBASE ]
    Pfam domain(s): Peripla_BP_1, HTH_AraC (2x)
    XylR is a member of the AraC family.

Additional/Linked Online Resources (top)

EcoCyc The link associated with each TF in the Notes section provides, in many cases, a graphical summary of the promoters/TUs regulated by the TF and other TFs that affect transcription of these promoters/TUs. The mode of action at each promoter (postive, negative, or dual) is indicated. Functional annotation is usually available by clicking on the name of a gene. Other information (e.g., synonyms, binding partners, enzymatic reactions catalyzed, references) is usually available.

EcoGene The link associated with each TF in the Notes section provides a fairly complete and current list of papers about the TF. Other information is available at the EcoGene site but is not directly accessible from a bibliography page (i.e., there are no links on these pages).

coliBASE The link associated with each TF in the Notes section provides a graphical view of the TF gene's genome context and other sequence-related information (e.g., a list of orthologs).

Pfam Links to annotation about Pfam domains are provided in the Notes section. Most Pfam domains were identified by HMM search using standard Pfam settings and the significance of the hits are above the gathering threshold. Click here for a list of the 50 TF protein sequences in FASTA format. Click here for the Pfam search results.

RegulonDB and Uri Alon's web site Each of these sites provides a fairly comprehensive list of TUs regulated by each of a large number of TFs in E. coli. If "others" appears in the Effector TU(s) column of a table entry, it is likely that additional information can be found at one of these sites.

PubMed Table entries are linked to PubMed abstracts. A list of full citations is provided in the pdf version of the table.

EcoTFs Updates of this table are planned. Check this site for the most recent version of the table and other information.

CellSignaling@LANL A gateway for information about systems biology research at Los Alamos National Laboratory in the area of cellular signaling.

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Last updated December 12, 2003