|Gene:||cnu||Accession Numbers: G6869 (EcoCyc), b1625, ECK1621|
YdgT (Cnu) is a paralog of the Hha protein and can partially compensate for the phenotypes of a hha mutant. YdgT interacts with H-NS and StpA and appears to protect StpA from proteolytic degradation [Paytubi04]. A heteromeric YdgT-H-NS complex binds the origin of replication (oriC) at a specific 26-bp sequence that overlaps a DnaA binding site [Kim05a].
A solution structure of YdgT has been determined. The H-NS binding site includes the flexible C-terminal region of YdgT [Bae08]. Residues important for the interaction with H-NS have been identified by random mutagenesis [Yun12a]. Expression of the K9E mutant leads to decreased DicA production, possibly by inhibiting DicA binding to its own promoter, and resulting in a temperature-dependent filamentous growth phenotype [Yun12].
YdgT expression is increased in a hha mutant background [Paytubi04]. Single ydgT or hha mutants show no effect on replication, but a ydgT hha double mutant has a slightly increased generation time [Kim05a]. In competitive growth experiments, a ydgT hha double mutant is outcompeted by wild type cells. The presence of pHly152 further lowers the competitive fitness of the ydgT hha double mutant; overexpression of H-NS suppresses the fitness defect [Aznar13]. A ydgT deletion mutant shows increased biofilm formation, while overexpression of ydgT leads to decreased biofilm formation [Hong10]. Overexpression of YdgT suppresses the transcriptional polarity relief phenotype of rho and nusG point mutants [Saxena11].
The transcriptome of a ydgT hha double mutant was compared to that of an hns stpA double mutant [Ueda13]. Microarray analysis of a ydgT mutant showed altered expression of a set of genes that overlapped significantly with genes whose expression was changed in a holE mutant [Dietrich13].
Cnu: "oriC-binding nucleoid-associated" [Kim05a]
|Map Position: [1,702,973 -> 1,703,188] (36.7 centisomes)||Length: 216 bp / 71 aa|
Molecular Weight of Polypeptide: 8.417 kD (from nucleotide sequence)
Unification Links: ASAP:ABE-0005443 , DIP:DIP-48011N , EchoBASE:EB4050 , EcoGene:EG14303 , EcoliWiki:b1625 , Mint:MINT-8175315 , ModBase:P64467 , OU-Microarray:b1625 , PortEco:cnu , PR:PRO_000022307 , Protein Model Portal:P64467 , RefSeq:NP_416142 , RegulonDB:G6869 , SMR:P64467 , String:511145.b1625 , Swiss-Model:P64467 , UniProt:P64467
|Biological Process:||GO:0060566 - positive regulation of DNA-templated transcription, termination
GO:1900232 - negative regulation of single-species biofilm formation on inanimate substrate [Hong10]
|Molecular Function:||GO:0005515 - protein binding
[deAlba11, Butland05, Paytubi04]
GO:0003677 - DNA binding [UniProtGOA11a]
|Cellular Component:||GO:0005829 - cytosol [DiazMejia09]|
|Growth Medium||Growth?||T (°C)||O2||pH||Osm/L||Growth Observations|
|LB enriched||Yes||37||Aerobic||6.95||Yes [Gerdes et al., 2003, Comment 1]|
|LB Lennox||Yes||37||Aerobic||7||Yes [Baba et al., 2006, Comment 2]|
|M9 medium with 1% glycerol||Yes||37||Aerobic||7.2||0.35||Yes [Joyce06, Comment 3]|
|MOPS medium with 0.4% glucose||Yes||37||Aerobic||7.2||0.22||Yes [Baba et al., 2006, Comment 2]|
Peter D. Karp on Thu Jan 16, 2003:
Predicted gene function revised as a result of E. coli genome reannotation by Serres et al. [Serres01 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.
Baba et al., 2006: 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
Bae08: Bae SH, Liu D, Lim HM, Lee Y, Choi BS (2008). "Structure of the nucleoid-associated protein Cnu reveals common binding sites for H-NS in Cnu and Hha." Biochemistry 47(7);1993-2001. PMID: 18189420
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
deAlba11: de Alba CF, Solorzano C, Paytubi S, Madrid C, Juarez A, Garcia J, Pons M (2011). "Essential residues in the H-NS binding site of Hha, a co-regulator of horizontally acquired genes in Enterobacteria." FEBS Lett 585(12);1765-70. PMID: 21600204
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
Dietrich13: Dietrich M, Pedro L, Garcia J, Pons M, Huttener M, Paytubi S, Madrid C, Juarez A (2013). "Evidence for moonlighting functions of the θ subunit of Escherichia coli DNA polymerase III." J Bacteriol. PMID: 24375106
Gerdes et al., 2003: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938
Hong10: Hong SH, Wang X, Wood TK (2010). "Controlling biofilm formation, prophage excision and cell death by rewiring global regulator H-NS of Escherichia coli." Microb Biotechnol 3(3);344-56. PMID: 21255333
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
Kim05a: Kim MS, Bae SH, Yun SH, Lee HJ, Ji SC, Lee JH, Srivastava P, Lee SH, Chae H, Lee Y, Choi BS, Chattoraj DK, Lim HM (2005). "Cnu, a novel oriC-binding protein of Escherichia coli." J Bacteriol 187(20);6998-7008. PMID: 16199570
Madrid07: Madrid C, Balsalobre C, Garcia J, Juarez A (2007). "The novel Hha/YmoA family of nucleoid-associated proteins: use of structural mimicry to modulate the activity of the H-NS family of proteins." Mol Microbiol 63(1);7-14. PMID: 17116239
Paytubi04: Paytubi S, Madrid C, Forns N, Nieto JM, Balsalobre C, Uhlin BE, Juarez A (2004). "YdgT, the Hha paralogue in Escherichia coli, forms heteromeric complexes with H-NS and StpA." Mol Microbiol 54(1);251-63. PMID: 15458420
Pedro11: Pedro L, Banos RC, Aznar S, Madrid C, Balsalobre C, Juarez A (2011). "Antibiotics shaping bacterial genome: deletion of an IS91 flanked virulence determinant upon exposure to subinhibitory antibiotic concentrations." PLoS One 6(11);e27606. PMID: 22096603
Srinivasan13: Srinivasan R, Chandraprakash D, Krishnamurthi R, Singh P, Scolari VF, Krishna S, Seshasayee AS (2013). "Genomic analysis reveals epistatic silencing of "expensive" genes in Escherichia coli K-12." Mol Biosyst 9(8);2021-33. PMID: 23661089
Ueda13: Ueda T, Takahashi H, Uyar E, Ishikawa S, Ogasawara N, Oshima T (2013). "Functions of the Hha and YdgT proteins in transcriptional silencing by the nucleoid proteins, H-NS and StpA, in Escherichia coli." DNA Res 20(3);263-71. PMID: 23543115
Yun12: Yun SH, Ji SC, Jeon HJ, Wang X, Kim SW, Bak G, Lee Y, Lim HM (2012). "The CnuK9E H-NS complex antagonizes DNA binding of DicA and leads to temperature-dependent filamentous growth in E. coli." PLoS One 7(9);e45236. PMID: 23028867
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