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

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

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1187939

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

About this item

Full title

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

Publisher

Chichester, UK: John Wiley & Sons, Ltd

Journal title

The EMBO journal, 2005-08, Vol.24 (16), p.2896-2905

Language

English

Formats

Publication information

Publisher

Chichester, UK: John Wiley & Sons, Ltd

More information

Scope and Contents

Contents

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...

Alternative Titles

Full title

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

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1187939

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1187939

Other Identifiers

ISSN

0261-4189

E-ISSN

1460-2075

DOI

10.1038/sj.emboj.7600754

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