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

Research output: Contribution to journalJournal articleResearchpeer-review

  • 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.

Original languageEnglish
JournalEMBO Journal
Volume24
Issue number16
Pages (from-to)2896-2905
Number of pages10
ISSN0261-4189
DOIs
Publication statusPublished - 17 Aug 2005

    Research areas

  • Protein dimerization and tetramerization, Transcriptional repression, Two-hybrid system

ID: 202333555