Structural highlights
4icg is a 4 chain structure with sequence from Saltu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| NonStd Res: | |
| Gene: | hns, hnsA, osmZ, STM1751, STMUK_1724 (SALTU), hha, STM0473, STMUK_0480 (SALTU) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[HNS_SALTY] H-NS binds tightly to ds-DNA, increases its thermal stability and inhibits transcription. It also binds to ss-DNA and RNA but with a much lower affinity. H-NS has possible histone-like function. May be a global transcriptional regulator through its ability to bind to curved DNA sequences, which are found in regions upstream of a certain subset of promoters. It plays a role in the thermal control of pili production. It is subject to transcriptional auto-repression. It binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150 (By similarity).
Publication Abstract from PubMed
The bacterial nucleoid associated proteins Hha and H-NS jointly repress horizontally acquired genes in Salmonella, including essential virulence loci encoded within Salmonella pathogenicity islands. Hha is known to interact with the N-terminal dimerization domain of H-NS, however the manner in which this interaction enhances transcriptional silencing is not understood. To further understand this process we solved the X-ray crystal structure of Hha in complex with the N-terminal dimerization domain of H-NS (H-NS1-46) to 3.2 A resolution. Two monomers of Hha bind to symmetrical sites on either side of the H-NS1-46 dimer. Disruption of the Hha/H-NS interaction by the H-NS site-specific mutation I11A, results in increased expression of the Hha/H-NS co-regulated gene hilA without affecting the expression levels of proV, a target gene repressed by H-NS in an Hha-independent fashion. Examination of the structure revealed a cluster of conserved basic amino acids that protrude from the surface of Hha on the opposite side of the Hha/H-NS1-46 interface. Hha mutants with a diminished positively charged surface maintain the ability to interact with H-NS but can no longer regulate hilA. Increased expression of the hilA locus did not correspond to significant depletion of H-NS at the promoter region in chromatin immunoprecipitation assays. However in vitro, we find Hha improves H-NS binding to target DNA fragments. Taken together, our results show for the first time how Hha and H-NS interact to direct transcriptional repression and reveal that a positively charged surface of Hha enhances the silencing activity of H-NS nucleoprotein filaments.
Structural Insights into the Regulation of Foreign Genes in Salmonella by the Hha/H-NS Complex.,Ali SS, Whitney JC, Stevenson J, Robinson H, Howell PL, Navarre WW J Biol Chem. 2013 Mar 20. PMID:23515315[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ali SS, Whitney JC, Stevenson J, Robinson H, Howell PL, Navarre WW. Structural Insights into the Regulation of Foreign Genes in Salmonella by the Hha/H-NS Complex. J Biol Chem. 2013 Mar 20. PMID:23515315 doi:10.1074/jbc.M113.455378
