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 for this work

Protein Structure and Function Program

46 Citations (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.

Original language	English
Journal	EMBO Journal
Volume	24
Issue number	16
Pages (from-to)	2896-2905
Number of pages	10
ISSN	0261-4189
DOIs	https://doi.org/10.1038/sj.emboj.7600754
Publication status	Published - 17 Aug 2005

Keywords

Protein dimerization and tetramerization
Transcriptional repression
Two-hybrid system

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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.",

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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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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.

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

Abstract

Keywords

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