|Gene:||sucB||Accession Numbers: EG10980 (EcoCyc), b0727, ECK0715|
Synonyms: E2(o) subunit
Component of: 2-oxoglutarate dehydrogenase complex (summary available)
Subunit composition of dihydrolipoyltranssuccinylase = [SucB]24
E. coli SucB is responsible for the dihydrolipoyltranssuccinylase (dihydrolipoamide succinyltransferase) activity of the 2-oxoglutarate dehydrogenase multienzyme complex (OGDHC) that catalyzes the conversion of 2-oxoglutarate (2-ketoglutarate) to succinyl-CoA and carbon dioxide, with the production of NADH (see 2-oxoglutarate decarboxylation to succinyl-CoA). SucB catalyzes the transfer of a succinyl group from the S-succinyldihydrolipoyl moiety to coenzyme A, forming succinyl-CoA.
The OGDHC is a member of the 2-oxo acid dehydrogenase family [Bunik08]. Members of this family contain multiple copies of three enzymatic components: 2-oxoglutarate decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). In most Gram-positive bacteria and in mitochondria the E1 component is a heterodimer composed of two subunits, while in most (but not all) Gram-negative bacteria it is made up of a single type of subunit. In both cases multiple copies of the E1 component along with multiple copies of the E3 component are assembled around an E2 core of 24 subunits with octahedral symmetry, or 60 subunits with eicosahedral symmetry (depending on which complex and species) [Reed01]. In E. coli the E3 component is shared with the pyruvate dehydrogenase and glycine cleavage multi-enzyme complexes. E1 and E2 differ slightly for the 2-oxoglutarate and pyruvate dehydrogenase complexes, and are designated (o) and (p) to distinguish them.
The E. coli OGDHC contains 12 units of the E1(o) component 2-oxoglutarate decarboxylase, thiamine-requiring encoded by sucA, 24 units of the E2(o) component dihydrolipoyltranssuccinylase encoded by sucB, and 2 units of the E3 component lipoamide dehydrogenase encoded by lpd. The 24 E2(o) units form the octahedral core of the complex. They contain lipoyllysine and binding sites for dimers of the E1(o) and E3 subunits. Electron cryotomography showed that they are flexibly tethered to the E2 core [Murphy05].
SucB has a single lipoyl domain at the N-terminus, and a domain with catalytic and subunit binding activity at the C-terminus. It also has areas that contain a large amount of alanine and proline [Spencer84]. The domain structure has been examined by limited proteolysis experiments [Packman87]. Data has suggested that E2(o) has a role in substrate specificity and channeling [Shim11, Perham02]. SucB is lipoylated by LipB, or LplA [Hassan11] (see the reactions below).
The crystal structure of the catalytic domain of SucB provided insights into its interaction with the lipoyl domain [Knapp00, Knapp98]. The crystal structure of the lipoyl domain has also been determined [Ricaud96]. This domain has also been studied by analysis of NMR spectra [Robien92, Ferguson05, Neuweiler09, Jones08].
SucB (E2(o)) has similarity to the AceF (E2(p)) subunit of the pyruvate dehydrogenase multienzyme complex although the N-terminal domain of AceF contains three lipoyl repeats, whereas SucB contains only one of these sequences [Spencer84]. E. coli SucB has similarity to Coxiella burnetii SucB, which elicits an immune response in infected humans [Nguyen99]. The Mycobacterium tuberculosis SucB is involved in a protective antioxidant response to attack by the immune system [Bryk02].
REACTION: E1(o) + TPP = E1(o).TPP, E1(o).TPP + 2-oxoglutarate = E1(o).hydroxycarboxypropylTPP + CO(2), E1(o).hydroxycarboxypropylTPP + E2(o).lipoate(S2) = E1(o).TPP + E2(o).lipoate(SH)(S-succinyl) (see [Waskiewicz84, Steginsky85])
The sucB gene was cloned and sequenced in earlier work [Spencer82, Spencer84] and the initial sequence of the gene was corrected [Packman87]. Transcription of the sucB gene has been analyzed in relation to other members of its gene cluster [Spencer85, Buck85, Buck86, Park97, Cunningham98a]. The sucAB and sucCD genes were shown to be mutually essential, with either pair sufficient to produce succinyl-CoA, but simultaneous deletion of sucAB and sucCD was not viable [Yu06c]. SucB and SucC were induced during growth at low pH [Stancik02]. Mutant studies showed that the sucB gene is involved in resistance to antibiotics and other stresses in a persister population of E. coli [Ma10].
|Map Position: [760,745 -> 761,962] (16.4 centisomes, 59°)||Length: 1218 bp / 405 aa|
Molecular Weight of Polypeptide: 44.011 kD (from nucleotide sequence)
Unification Links: ASAP:ABE-0002480 , CGSC:145 , DIP:DIP-35787N , EchoBASE:EB0973 , EcoGene:EG10980 , EcoliWiki:b0727 , Mint:MINT-1242608 , OU-Microarray:b0727 , PortEco:sucB , PR:PRO_000024003 , Pride:P0AFG6 , Protein Model Portal:P0AFG6 , RegulonDB:EG10980 , SMR:P0AFG6 , String:511145.b0727 , Swiss-Model:P0AFG6 , UniProt:P0AFG6
Relationship Links: InterPro:IN-FAMILY:IPR000089 , InterPro:IN-FAMILY:IPR001078 , InterPro:IN-FAMILY:IPR003016 , InterPro:IN-FAMILY:IPR004167 , InterPro:IN-FAMILY:IPR006255 , InterPro:IN-FAMILY:IPR011053 , InterPro:IN-FAMILY:IPR023213 , PDB:Structure:1BAL , PDB:Structure:1BBL , PDB:Structure:1C4T , PDB:Structure:1E2O , PDB:Structure:1PMR , PDB:Structure:1SCZ , PDB:Structure:1W4H , PDB:Structure:2BTG , PDB:Structure:2BTH , PDB:Structure:2WXC , Pfam:IN-FAMILY:PF00198 , Pfam:IN-FAMILY:PF00364 , Pfam:IN-FAMILY:PF02817 , Prosite:IN-FAMILY:PS00189 , Prosite:IN-FAMILY:PS50968
In Paralogous Gene Group: 39 (2 members)
Reactions known to consume the compound:
Not in pathways:
ATP + SucB + (R)-lipoate → AMP + SucB-lipoate + diphosphate
In Reactions of unknown directionality:
Not in pathways:
SucB + lipoyl-ACP = SucB-lipoate + a holo-[acyl-carrier protein]
Instance reactions of [a [lipoyl-carrier protein] N6-dihydrolipoyl-L-lysine + NAD+ = a [lipoyl-carrier protein] N6-lipoyl-L-lysine + NADH + H+] (220.127.116.11):
|Biological Process:||GO:0006099 - tricarboxylic acid cycle
[UniProtGOA11a, GOA01a, Spencer82]
GO:0008152 - metabolic process [GOA01a]
GO:0033512 - L-lysine catabolic process to acetyl-CoA via saccharopine [UniProtGOA12]
|Molecular Function:||GO:0004149 - dihydrolipoyllysine-residue succinyltransferase activity
[GOA01, GOA01a, Spencer82, Willms67]
GO:0005515 - protein binding [Rajagopala14, Butland05]
GO:0031405 - lipoic acid binding [Packman91]
GO:0016740 - transferase activity [UniProtGOA11a]
GO:0016746 - transferase activity, transferring acyl groups [UniProtGOA11a, GOA01a]
|Cellular Component:||GO:0005829 - cytosol
[DiazMejia09, Ishihama08, Molloy00, LopezCampistrou05]
GO:0045252 - oxoglutarate dehydrogenase complex [GOA01a, Willms67]
|MultiFun Terms:||metabolism → energy metabolism, carbon → TCA cycle|
|Growth Medium||Growth?||T (°C)||O2||pH||Osm/L||Growth Observations|
|LB Lennox||Yes||37||Aerobic||7||Yes [Baba06, Comment 1]|
|M9 medium with 1% glycerol||Yes||37||Aerobic||7.2||0.35||Yes [Joyce06, Comment 2]|
|MOPS medium with 0.4% glucose||Yes||37||Aerobic||7.2||0.22||Yes [Baba06, Comment 1] |
Yes [Feist07, Comment 3]
Enzymatic reaction of: dihydrolipoyltranssuccinylase
Synonyms: lipoate succinyltransferase, dihydrolipoamide succinyltransferase, lipoamide acyltransferase
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.
The reaction is physiologically favored in the direction shown.
In Pathways: 2-oxoglutarate decarboxylation to succinyl-CoA
Subunit of: 2-oxoglutarate dehydrogenase complex
Subunit composition of
2-oxoglutarate dehydrogenase complex = [(SucA)12][(SucB)24][(Lpd)2]
2-oxoglutarate decarboxylase, thiamine-requiring = (SucA)12 (extended summary available)
subunit of E1(0) component of 2-oxoglutarate dehydrogenase = SucA
dihydrolipoyltranssuccinylase = (SucB)24 (extended summary available)
lipoamide dehydrogenase = (Lpd)2 (extended summary available)
E3 monomer = Lpd
The 2-oxoglutarate (2-ketoglutarate) dehydrogenase complex is similar in enzyme composition and complex reactions to the pyruvate dehydrogenase complex reactions [Perham87, Stephens83, Perham89] (see 2-oxoglutarate decarboxylation to succinyl-CoA and pyruvate decarboxylation to acetyl CoA).
SUBREACTIONS: E1(o) + TPP = E1(o).TPP E1(o).TPP + succinate = E1(o).hydroxycarboxypropylTPP + CO(2) E1(o).hydroxycarboxypropylTPP + E2(o).lipoate(S2) = E1(o).TPP + E2(o).lipoate(SH)(S-succinyl) E2(o).lipoate(SH)(S-succinyl) + CoA = E2(o).lip(SH)2 + succinylCoA E3 + FAD = E3.FAD E3.FAD + E2(o).lip(SH)2 = E3.FADH(2) + E2(o).lip(S)2 E3.FADH(2) + NAD(+) = E3.FAD + NADH + H(+) (see [Steginsky85, Waskiewicz84].
Enzymatic reaction of: 2-oxoglutarate dehydrogenase
Synonyms: α-ketoglutarate dehydrogenase, 2-ketoglutarate dehydrogenase
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is favored in the direction shown.
In Pathways: 2-oxoglutarate decarboxylation to succinyl-CoA , superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass , superpathway of glyoxylate bypass and TCA , TCA cycle I (prokaryotic)
The [Waskiewicz84] data are for E. coli B.
|Chain||2 -> 405|
|Conserved-Region||3 -> 78|
10/20/97 Gene b0727 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10980; confirmed by SwissProt match.
Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554
Bryk02: Bryk R, Lima CD, Erdjument-Bromage H, Tempst P, Nathan C (2002). "Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein." Science 295(5557);1073-7. PMID: 11799204
Buck89: Buck D, Guest JR (1989). "Overexpression and site-directed mutagenesis of the succinyl-CoA synthetase of Escherichia coli and nucleotide sequence of a gene (g30) that is adjacent to the suc operon." Biochem J 1989;260(3);737-47. PMID: 2548486
Bunik08: Bunik VI, Degtyarev D (2008). "Structure-function relationships in the 2-oxo acid dehydrogenase family: substrate-specific signatures and functional predictions for the 2-oxoglutarate dehydrogenase-like proteins." Proteins 71(2);874-90. PMID: 18004749
Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909
Ferguson05: Ferguson N, Sharpe TD, Schartau PJ, Sato S, Allen MD, Johnson CM, Rutherford TJ, Fersht AR (2005). "Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family." J Mol Biol 353(2);427-46. PMID: 16168437
Frank07: Frank RA, Price AJ, Northrop FD, Perham RN, Luisi BF (2007). "Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex." J Mol Biol 368(3);639-51. PMID: 17367808
Jones08: Jones DD, Perham RN (2008). "The role of loop and beta-turn residues as structural and functional determinants for the lipoyl domain from the Escherichia coli 2-oxoglutarate dehydrogenase complex." Biochem J 409(2);357-66. PMID: 17927566
Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394
Knapp00: Knapp JE, Carroll D, Lawson JE, Ernst SR, Reed LJ, Hackert ML (2000). "Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase." Protein Sci 9(1);37-48. PMID: 10739245
Knapp98: Knapp JE, Mitchell DT, Yazdi MA, Ernst SR, Reed LJ, Hackert ML (1998). "Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex." J Mol Biol 280(4);655-68. PMID: 9677295
Lindsay00: Lindsay H, Beaumont E, Richards SD, Kelly SM, Sanderson SJ, Price NC, Lindsay JG (2000). "FAD insertion is essential for attaining the assembly competence of the dihydrolipoamide dehydrogenase (E3) monomer from Escherichia coli." J Biol Chem 275(47);36665-70. PMID: 10970889
Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646
LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532
Ma10: Ma C, Sim S, Shi W, Du L, Xing D, Zhang Y (2010). "Energy production genes sucB and ubiF are involved in persister survival and tolerance to multiple antibiotics and stresses in Escherichia coli." FEMS Microbiol Lett 303(1);33-40. PMID: 20041955
Magnusson86: Magnusson K, Philips MK, Guest JR, Rutberg L (1986). "Nucleotide sequence of the gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex." J Bacteriol 1986;166(3);1067-71. PMID: 3086287
Molloy00: Molloy MP, Herbert BR, Slade MB, Rabilloud T, Nouwens AS, Williams KL, Gooley AA (2000). "Proteomic analysis of the Escherichia coli outer membrane." Eur J Biochem 267(10);2871-81. PMID: 10806384
Neuweiler09: Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR (2009). "The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family." J Mol Biol 390(5);1060-73. PMID: 19445954
Nguyen99: Nguyen SV, To H, Yamaguchi T, Fukushi H, Hirai K (1999). "Characterization of the Coxiella burnetti sucB gene encoding an immunogenic dihydrolipoamide succinyltransferase." Microbiol Immunol 43(8);743-9. PMID: 10524791
Packman87: Packman LC, Perham RN (1987). "Limited proteolysis and sequence analysis of the 2-oxo acid dehydrogenase complexes from Escherichia coli. Cleavage sites and domains in the dihydrolipoamide acyltransferase components." Biochem J 242(2);531-8. PMID: 3297046
Packman91: Packman LC, Green B, Perham RN (1991). "Lipoylation of the E2 components of the 2-oxo acid dehydrogenase multienzyme complexes of Escherichia coli." Biochem J 277 ( Pt 1);153-8. PMID: 1854331
Park97: Park SJ, Chao G, Gunsalus RP (1997). "Aerobic regulation of the sucABCD genes of Escherichia coli, which encode alpha-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream sdhCDAB promoter." J Bacteriol 179(13);4138-42. PMID: 9209026
Pettit73: Pettit FH, Hamilton L, Munk P, Namihira G, Eley MH, Willms CR, Reed LJ (1973). "Alpha-keto acid dehydrogenase complexes. XIX. Subunit structure of the Escherichia coli alpha-ketoglutarate dehydrogenase complex." J Biol Chem 248(15);5282-90. PMID: 4588679
Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554
Ricaud96: Ricaud PM, Howard MJ, Roberts EL, Broadhurst RW, Perham RN (1996). "Three-dimensional structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli." J Mol Biol 264(1);179-90. PMID: 8950276
Robien92: Robien MA, Clore GM, Omichinski JG, Perham RN, Appella E, Sakaguchi K, Gronenborn AM (1992). "Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli." Biochemistry 31(13);3463-71. PMID: 1554728
Shim11: Shim da J, Nemeria NS, Balakrishnan A, Patel H, Song J, Wang J, Jordan F, Farinas ET (2011). "Assignment of function to histidines 260 and 298 by engineering the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase complex; substitutions that lead to acceptance of substrates lacking the 5-carboxyl group." Biochemistry 50(35);7705-9. PMID: 21809826
Spencer84: Spencer ME, Darlison MG, Stephens PE, Duckenfield IK, Guest JR (1984). "Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase." Eur J Biochem 141(2);361-74. PMID: 6376124
Stancik02: Stancik LM, Stancik DM, Schmidt B, Barnhart DM, Yoncheva YN, Slonczewski JL (2002). "pH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli." J Bacteriol 184(15);4246-58. PMID: 12107143
Steginsky85: Steginsky CA, Gruys KJ, Frey PA (1985). "alpha-Ketoglutarate dehydrogenase complex of Escherichia coli. A hybrid complex containing pyruvate dehydrogenase subunits from pyruvate dehydrogenase complex." J Biol Chem 260(25);13690-3. PMID: 3902822
Stephens83: Stephens PE, Darlison MG, Lewis HM, Guest JR (1983). "The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component." Eur J Biochem 1983;133(3);481-9. PMID: 6345153
Waskiewicz84: Waskiewicz DE, Hammes GG (1984). "Elementary steps in the reaction mechanism of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: kinetics of succinylation and desuccinylation." Biochemistry 23(14);3136-43. PMID: 6380583
Willms67: Willms CR, Oliver RM, Henney HR, Mukherjee BB, Reed LJ (1967). "Alpha-keto acid dehydrogenase complexes. VI. Dissociation and reconstitution of the dihydrolipoyl transacetylase of Escherichia coli." J Biol Chem 242(5);889-97. PMID: 5335914
Wood84: Wood D, Darlison MG, Wilde RJ, Guest JR (1984). "Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli." Biochem J 1984;222(2);519-34. PMID: 6383359
Zhang09a: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842
Iuchi88: Iuchi S, Lin EC (1988). "arcA (dye), a global regulatory gene in Escherichia coli mediating repression of enzymes in aerobic pathways." Proc Natl Acad Sci U S A 1988;85(6);1888-92. PMID: 2964639
Kumar11: Kumar R, Shimizu K (2011). "Transcriptional regulation of main metabolic pathways of cyoA, cydB, fnr, and fur gene knockout Escherichia coli in C-limited and N-limited aerobic continuous cultures." Microb Cell Fact 10;3. PMID: 21272324
Lynch96: Lynch AS, Lin EC (1996). "Transcriptional control mediated by the ArcA two-component response regulator protein of Escherichia coli: characterization of DNA binding at target promoters." J Bacteriol 1996;178(21);6238-49. PMID: 8892825
Park95: Park SJ, Tseng CP, Gunsalus RP (1995). "Regulation of succinate dehydrogenase (sdhCDAB) operon expression in Escherichia coli in response to carbon supply and anaerobiosis: role of ArcA and Fnr." Mol Microbiol 15(3);473-82. PMID: 7783618
Salmon05: Salmon KA, Hung SP, Steffen NR, Krupp R, Baldi P, Hatfield GW, Gunsalus RP (2005). "Global gene expression profiling in Escherichia coli K12: effects of oxygen availability and ArcA." J Biol Chem 280(15);15084-96. PMID: 15699038
Shen97: Shen J, Gunsalus RP (1997). "Role of multiple ArcA recognition sites in anaerobic regulation of succinate dehydrogenase (sdhCDAB) gene expression in Escherichia coli." Mol Microbiol 26(2);223-36. PMID: 9383149
Trotter11: Trotter EW, Rolfe MD, Hounslow AM, Craven CJ, Williamson MP, Sanguinetti G, Poole RK, Green J (2011). "Reprogramming of Escherichia coli K-12 metabolism during the initial phase of transition from an anaerobic to a micro-aerobic environment." PLoS One 6(9);e25501. PMID: 21980479
Wright13: Wright PR, Richter AS, Papenfort K, Mann M, Vogel J, Hess WR, Backofen R, Georg J (2013). "Comparative genomics boosts target prediction for bacterial small RNAs." Proc Natl Acad Sci U S A 110(37);E3487-96. PMID: 23980183
Zhang05: Zhang Z, Gosset G, Barabote R, Gonzalez CS, Cuevas WA, Saier MH (2005). "Functional interactions between the carbon and iron utilization regulators, Crp and Fur, in Escherichia coli." J Bacteriol 187(3);980-90. PMID: 15659676
Zheng04: Zheng D, Constantinidou C, Hobman JL, Minchin SD (2004). "Identification of the CRP regulon using in vitro and in vivo transcriptional profiling." Nucleic Acids Res 32(19);5874-93. PMID: 15520470
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