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Nature and mechanism of the in vivo oligomerization of nucleoid protein H-NS

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  • Stella, Stefano
  • Roberto Spurio
  • Maurizio Falconi
  • Cynthia L. Pon
  • Claudio O. Gualerzi

Two types of two-hybrid systems demonstrate that the transcriptional repressor, nucleoid-associated protein H-NS (histone-like, nucleoid structuring protein) forms dimers and tetramers in vivo, the latter being the active form of the protein. The H-NS 'protein oligomerization' domain (N-domain) is unable to oligomerize in the absence of the intradomain linker while the 'DNA-binding' C-domain clearly displays a protein-protein interaction capacity, which contributes to H-NS tetramerization and which is lost following Pro115 mutation. Linker deletion or substitution with KorB linker abolishes H-NS oligomerization. A model describing H-NS dimerization and tetramerization based on all available data and suggesting the existence in the tetramer of a bundle of four α-helices, each contributed by an H-NS monomer, is presented.

OriginalsprogEngelsk
TidsskriftEMBO Journal
Vol/bind24
Udgave nummer16
Sider (fra-til)2896-2905
Antal sider10
ISSN0261-4189
DOI
StatusUdgivet - 17 aug. 2005

ID: 202333555