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

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

doi:10.1038/sj.emboj.7600754

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

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

^*Corresponding author af dette arbejde

Protein Structure and Function Program

46 Citationer (Scopus)

Abstract

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.

Originalsprog	Engelsk
Tidsskrift	EMBO Journal
Vol/bind	24
Udgave nummer	16
Sider (fra-til)	2896-2905
Antal sider	10
ISSN	0261-4189
DOI	https://doi.org/10.1038/sj.emboj.7600754
Status	Udgivet - 17 aug. 2005

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AU - Spurio, Roberto

AU - Falconi, Maurizio

AU - Pon, Cynthia L.

AU - Gualerzi, Claudio O.

PY - 2005/8/17

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N2 - 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.

AB - 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.

KW - Protein dimerization and tetramerization

KW - Transcriptional repression

KW - Two-hybrid system

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

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