Transcription Factor

						

			
Accessions: ECK120004670 (RegulonDB 7.5)

			
Names: CytR
Organisms: ECK12
Libraries: RegulonDB 7.5 1
1 Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muniz-Rascado L, Garcia-Sotelo JS, Weiss V, Solano-Lira H, Martinez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernandez S, Alquicira-Hernandez K, Lopez-Fuentes A, Porron-Sotelo L, Huerta AM, Bonavides-Martinez C, Balderas-Martinez YI, Pannier L, Olvera M, Labastida A, Jimenez-Jacinto V, Vega-Alvarado L, Del Moral-Chavez V, Hernandez-Alvarez A, Morett E, Collado-Vides J. RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more. Nucleic Acids Res. 2013 Jan 1;41(D1):D203-D213. [Pubmed]
Notes: nucleotide and nucleoside conversions; cytoplasm; repressor; activator; regulon; regulation of nucleobase-containing compound metabolic process; regulation of transcription, DNA-dependent; intracellular; protein binding; sequence-specific DNA binding transcription factor activity; DNA binding; transcription activator activity; transcription, DNA-dependent; transcription repressor activity; Transcription related
Length: 342
Pfam Domains:     11-56 Bacterial regulatory proteins, lacI family
   68-315 Periplasmic binding proteins and sugar binding domain of LacI family
   70-318 Periplasmic binding protein domain
  176-337 Periplasmic binding protein-like domain
Sequence: 
(in bold interface residues)		   1 VKAKKQETAATMKDVALKAKVSTATVSRALMNPDKVSQATRNRVEKAAREVGYLPQPMGR   60
  61 NVKRNESRTILVIVPDICDPFFSEIIRGIEVTAANHGYLVLIGDCAHQNQQEKTFIDLII  120
 121 TKQIDGMLLLGSRLPFDASIEEQRNLPPMVMANEFAPELELPTVHIDNLTAAFDAVNYLY  180
 181 EQGHKRIGCIAGPEEMPLCHYRLQGYVQALRRCGIMVDPQYIARGDFTFEAGSKAMQQLL  240
 241 DLPQPPTAVFCHSDVMALGALSQAKRQGLKVPEDLSIIGFDNIDLTQFCDPPLTTIAQPR  300
 301 YEIGREAMLLLLDQMQGQHVGSGSRLMDCELIIRGSTRALP*
Interface Residues: 12, 13, 22, 23, 24, 25, 27, 28, 34, 35, 36, 59, 62, 63, 135, 145
3D-footprint Homologues: 7ce1_D, 1efa_B, 3oqm_C, 1l1m_B, 1zvv_A, 1jft_A, 3k59_A
Binding Motifs: CytR whwdKtwTGCAAwbkdtt
Binding Sites: ECK120012675
ECK120013078
ECK120013396
ECK120013444
ECK120013448
ECK120013485
ECK120013543
ECK120013557
ECK120013655
ECK120016528
ECK125108588
ECK125108590
ECK125108592
ECK125108595
ECK125108597
ECK125108601
ECK125108603
ECK125108605
ECK125108609
ECK125108637
ECK125108639
			
Publications: Valentin-Hansen P., Sogaard-Andersen L., Pedersen H. A flexible partnership: the CytR anti-activator and the cAMP-CRP activator protein, comrades in transcription control. Mol Microbiol. 20(3):461-6 (1996). [Pubmed]


Perini LT., Doherty EA., Werner E., Senear DF. Multiple specific CytR binding sites at the Escherichia coli deoP2 promoter mediate both cooperative and competitive interactions between CytR and cAMP receptor protein. J Biol Chem. 271(52):33242-55 (1996). [Pubmed]


Kallipolitis BH., Valentin-Hansen P. Transcription of rpoH, encoding the Escherichia coli heat-shock regulator sigma32, is negatively controlled by the cAMP-CRP/CytR nucleoprotein complex. Mol Microbiol. 29(4):1091-9 (1998). [Pubmed]


Norregaard-Madsen M., Mygind B., Pedersen R., Valentin-Hansen P., Sogaard-Andersen L. The gene encoding the periplasmic cyclophilin homologue, PPIase A, in Escherichia coli, is expressed from four promoters, three of which are activated by the cAMP-CRP complex and negatively regulated by the CytR repressor. Mol Microbiol. 14(5):989-97 (1994). [Pubmed]


Muller-Hill B. Some repressors of bacterial transcription. Curr Opin Microbiol. 1(2):145-51 (1998). [Pubmed]


Pedersen H., Sogaard-Andersen L., Holst B., Gerlach P., Bremer E., Valentin-Hansen P. cAMP-CRP activator complex and the CytR repressor protein bind co-operatively to the cytRP promoter in Escherichia coli and CytR antagonizes the cAMP-CRP-induced DNA bend. J Mol Biol. 227(2):396-406 (1992). [Pubmed]


Gerlach P., Valentin-Hansen P., Bremer E. Transcriptional regulation of the cytR repressor gene of Escherichia coli: autoregulation and positive control by the cAMP/CAP complex. Mol Microbiol. 4(3):479-88 (1990). [Pubmed]


Moody CL., Tretyachenko-Ladokhina V., Laue TM., Senear DF., Cocco MJ. Multiple Conformations of the Cytidine Repressor DNA-Binding Domain Coalesce to One upon Recognition of a Specific DNA Surface. Biochemistry. 50(31):6622-32 (2011). [Pubmed]


Kallipolitis BH., Norregaard-Madsen M., Valentin-Hansen P. Protein-protein communication: structural model of the repression complex formed by CytR and the global regulator CRP. Cell. 89(7):1101-9 (1997). [Pubmed]


Weickert MJ., Adhya S. A family of bacterial regulators homologous to Gal and Lac repressors. J Biol Chem. 267(22):15869-74 (1992). [Pubmed]


Pedersen H., Dall J., Dandanell G., Valentin-Hansen P. Gene-regulatory modules in Escherichia coli: nucleoprotein complexes formed by cAMP-CRP and CytR at the nupG promoter. Mol Microbiol. 17(5):843-53 (1995). [Pubmed]


Craig JE., Zhang Y., Gallagher MP. Cloning of the nupC gene of Escherichia coli encoding a nucleoside transport system, and identification of an adjacent insertion element, IS 186. Mol Microbiol. 11(6):1159-68 (1994). [Pubmed]


Gerlach P., Sogaard-Andersen L., Pedersen H., Martinussen J., Valentin-Hansen P., Bremer E. The cyclic AMP (cAMP)-cAMP receptor protein complex functions both as an activator and as a corepressor at the tsx-p2 promoter of Escherichia coli K-12. J Bacteriol. 173(17):5419-30 (1991). [Pubmed]


Jorgensen CI., Kallipolitis BH., Valentin-Hansen P. DNA-binding characteristics of the Escherichia coli CytR regulator: a relaxed spacing requirement between operator half-sites is provided by a flexible, unstructured interdomain linker. Mol Microbiol. 27(1):41-50 (1998). [Pubmed]


Zolotukhina M., Ovcharova I., Eremina S., Errais Lopes L., Mironov AS. Comparison of the structure and regulation of the udp gene of Vibrio cholerae, Yersinia pseudotuberculosis, Salmonella typhimurium, and Escherichia coli. Res Microbiol. 154(7):510-20 (2003). [Pubmed]


Meibom KL., Kallipolitis BH., Ebright RH., Valentin-Hansen P. Identification of the subunit of cAMP receptor protein (CRP) that functionally interacts with CytR in CRP-CytR-mediated transcriptional repression. J Biol Chem. 275(16):11951-6 (2000). [Pubmed]


Kristensen HH., Valentin-Hansen P., Sogaard-Andersen L. Design of CytR regulated, cAMP-CRP dependent class II promoters in Escherichia coli: RNA polymerase-promoter interactions modulate the efficiency of CytR repression. J Mol Biol. 266(5):866-76 (1997). [Pubmed]


Meibom KL., Sogaard-Andersen L., Mironov AS., Valentin-Hansen P. Dissection of a surface-exposed portion of the cAMP-CRP complex that mediates transcription activation and repression. Mol Microbiol. 32(3):497-504 (1999). [Pubmed]


Kristensen HH., Valentin-Hansen P., Sogaard-Andersen L. CytR/cAMP-CRP nucleoprotein formation in E. coli: the CytR repressor binds its operator as a stable dimer in a ternary complex with cAMP-CRP. J Mol Biol. 260(2):113-9 (1996). [Pubmed]


Rasmussen PB., Holst B., Valentin-Hansen P. Dual-function regulators: the cAMP receptor protein and the CytR regulator can act either to repress or to activate transcription depending on the context. Proc Natl Acad Sci U S A. 93(19):10151-5 (1996). [Pubmed]


Sogaard-Andersen L., Mollegaard NE., Douthwaite SR., Valentin-Hansen P. Tandem DNA-bound cAMP-CRP complexes are required for transcriptional repression of the deoP2 promoter by the CytR repressor in Escherichia coli. Mol Microbiol. 4(9):1595-601 (1990). [Pubmed]


Sogaard-Andersen L., Martinussen J., Mollegaard NE., Douthwaite SR., Valentin-Hansen P. The CytR repressor antagonizes cyclic AMP-cyclic AMP receptor protein activation of the deoCp2 promoter of Escherichia coli K-12. J Bacteriol. 172(10):5706-13 (1990). [Pubmed]


Sogaard-Andersen L., Pedersen H., Holst B., Valentin-Hansen P. A novel function of the cAMP-CRP complex in Escherichia coli: cAMP-CRP functions as an adaptor for the CytR repressor in the deo operon. Mol Microbiol. 5(4):969-75 (1991). [Pubmed]


Pedersen H., Sogaard-Andersen L., Holst B., Valentin-Hansen P. Heterologous cooperativity in Escherichia coli. The CytR repressor both contacts DNA and the cAMP receptor protein when binding to the deoP2 promoter. J Biol Chem. 266(27):17804-8 (1991). [Pubmed]


Gavigan SA., Nguyen T., Nguyen N., Senear DF. Role of multiple CytR binding sites on cooperativity, competition, and induction at the Escherichia coli udp promoter. J Biol Chem. 274(23):16010-9 (1999). [Pubmed]


Pedersen H., Valentin-Hansen P. Protein-induced fit: the CRP activator protein changes sequence-specific DNA recognition by the CytR repressor, a highly flexible LacI member. EMBO J. 16(8):2108-18 (1997). [Pubmed]


Kallipolitis BH., Valentin-Hansen P. A role for the interdomain linker region of the Escherichia coli CytR regulator in repression complex formation. J Mol Biol. 342(1):1-7 (2004). [Pubmed]
Related annotations: PaperBLAST

	
			


			

				

				
				
				
				

			

			

		

	
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