Notes For:
YdgT (Cnu) is a paralog of the |FRAME: EG10439-MONOMER 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 |CITS: [15458420]|. A heteromeric YdgT-H-NS complex binds the origin of replication (|FRAME: G0-10506 oriC|) at a specific 26-bp sequence that overlaps a DnaA binding site |CITS: [16199570]|.
Both YdgT and HolE appear to influence expression of |FRAME: EG11005 tnaA| by enhancing transcription termination at the leader DNA sequence |CITS: [24375106]|.
A solution structure of YdgT has been determined. The H-NS binding site includes the flexible C-terminal region of YdgT |CITS: [18189420]|. Residues important for the interaction with H-NS have been identified by random mutagenesis |CITS: [22358512]|. 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 |CITS: [23028867]|.
YdgT expression is increased in a hha mutant background |CITS: [15458420]|. Single ydgT or hha mutants show no effect on replication, but a ydgT hha double mutant has a slightly increased generation time |CITS: [16199570]|. 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 |CITS: [23258263]|. A ydgT deletion mutant shows increased biofilm formation, while overexpression of ydgT leads to decreased biofilm formation |CITS: [21255333]|. Overexpression of YdgT suppresses the transcriptional polarity relief phenotype of rho and nusG point mutants |CITS: [21602341]|.
The transcriptome of a ydgT hha double mutant was compared to that of an hns stpA double mutant |CITS: [23543115]|. 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 |CITS: [24375106]|.
Cnu: oriC-binding nucleoid-associated |CITS: [16199570]|
Review: |CITS: [17116239]|
Reference(s): |
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[1] 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 |
[2] 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 |
[3] Dietrich M, Pedró L, García J, Pons M, Hüttener M, Paytubi S, Madrid C, Juárez A, 2014, Evidence for moonlighting functions of the ? subunit of Escherichia coli DNA polymerase III., J Bacteriol, 196(5):1102 10.1128/JB.01448-13 |
[4] 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 10.1093/dnares/dst008 |
[5] Saxena S., Gowrishankar J., 2011, Modulation of Rho-dependent transcription termination in Escherichia coli by the H-NS family of proteins., J Bacteriol 193(15):3832-41 |
[6] 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 |
[7] 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 |
[8] 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 |
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