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.
Nature and mechanism of the in vivo oligomerizzation of nucleoid protein H-NS / STELLA S.; SPURIO R.; FALCONI M.; PON CL; GUALERZI CO. - In: EMBO JOURNAL. - ISSN 0261-4189. - STAMPA. - 24:16(2005), pp. 2896-2905.
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Titolo: | Nature and mechanism of the in vivo oligomerizzation of nucleoid protein H-NS |
Autori: | |
Data di pubblicazione: | 2005 |
Rivista: | |
Citazione: | Nature and mechanism of the in vivo oligomerizzation of nucleoid protein H-NS / STELLA S.; SPURIO R.; FALCONI M.; PON CL; GUALERZI CO. - In: EMBO JOURNAL. - ISSN 0261-4189. - STAMPA. - 24:16(2005), pp. 2896-2905. |
Handle: | http://hdl.handle.net/11581/115475 |
Appare nelle tipologie: | Articolo |