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) |
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.
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).
AsnC [ Table Entry | EcoCyc
| EcoGene
| coliBASE | PDB BLAST (NCBI)
]
Pfam domain(s): AsnC_trans_reg
AsnC is a member of the AsnC/Lrp family.
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.
CpxR [ Table Entry | EcoCyc
| EcoGene
| coliBASE
| PDB BLAST (NCBI)
]
Pfam domain(s): Response_reg,
Trans_reg_C
CynR [ Table Entry | EcoCyc
| EcoGene
| coliBASE | PDB BLAST (NCBI)
]
Pfam domain(s): HTH_1,
LysR_substrate
CynR is a member of the LysR family.
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).
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.
DnaA [ Table Entry | EcoCyc
| EcoGene
| coliBASE | PDB BLAST (NCBI)
]
Pfam domain(s): Bac_DnaA
DnaA is a bacterial dnaA protein.
DsdC [ Table Entry | EcoCyc
| EcoGene
| coliBASE | PDB BLAST (NCBI)
]
Pfam domain(s): HTH_1,
LysR_substrate
DsdC is a member of the LysR family.
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.
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.
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.
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.
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.
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.
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.
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.
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.
H-NS [ Table Entry | EcoCyc
| EcoGene
| coliBASE
]
Pfam domain(s): Histone_HNS
H-NS is a histone-like nucleoid-structuring protein.
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.
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).
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).
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.
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).
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.
MarR [ Table Entry | EcoCyc
| EcoGene
| coliBASE | PDB BLAST (NCBI)
]
Pfam domain(s): MarR
MarR is a member of the MarR family.
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.
MelR [ Table Entry | EcoCyc
| EcoGene
| coliBASE | PDB BLAST (NCBI)
]
Pfam domain(s): HTH_AraC
(2x)
MelR is a member of the AraC family?
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).
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).
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.
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).
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)
PdhR [ Table Entry | EcoCyc
| EcoGene
| coliBASE | PDB BLAST (NCBI)
]
Pfam domain(s): GntR
PdhR is a member of the GntR family. pdhR=genA
PspF [ Table Entry | EcoCyc
| EcoGene
| coliBASE | PDB BLAST (NCBI)
]
Pfam domain(s): Sigma54_activat
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.
PutA [ Table Entry | EcoCyc
| EcoGene
| coliBASE | PDB BLAST (NCBI)
]
Pfam domain(s): Pro_dh,
Aldedh
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.
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.
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.
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.
SoxR [ Table Entry | EcoCyc
| EcoGene
| coliBASE | PDB BLAST (NCBI)
]
Pfam domain(s): MerR
SoxR is a member of the MerR family.
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.
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).
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.
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.
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.
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).
XapR [ Table Entry | EcoCyc
| EcoGene
| coliBASE | PDB BLAST (NCBI)
]
Pfam domain(s): HTH_1,
LysR_substrate
XapR is a member of the LysR family.
XylR [ Table Entry | EcoCyc
| EcoGene
| coliBASE
]
Pfam domain(s): Peripla_BP_1,
HTH_AraC
(2x)
XylR is a member of the AraC family.