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SNASP, a histone H1-specific eukaryotic chaperone dimer that facilitates chromatin assembly.

ABSTRACT: NASP has been described as a histone H1 chaperone in mammals. However, the molecular mechanisms involved have not yet been characterized. Here, we show that this protein is not only present in mammals but is widely distributed throughout eukaryotes both in its somatic and testicular forms. The secondary structure of the human somatic version consists mainly of clusters of alpha-helices and exists as a homodimer in solution. The protein binds nonspecifically to core histone H2A-H2B dimers and H3-H4 tetramers but only forms specific complexes with histone H1. The formation of the NASP-H1 complexes is mediated by the N- and C-terminal domains of histone H1 and does not involve the winged helix domain that is characteristic of linker histones. In vitro chromatin reconstitution experiments show that this protein facilitates the incorporation of linker histones onto nucleosome arrays and hence is a bona fide linker histone chaperone.

SUBMITTER: Finn RM

PROVIDER: S-EPMC2479616 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature

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sNASP, a histone H1-specific eukaryotic chaperone dimer that facilitates chromatin assembly.

Finn Ron M RM Browne Kristen K Hodgson Kim C KC Ausió Juan J

Biophysical journal 20080502 3

NASP has been described as a histone H1 chaperone in mammals. However, the molecular mechanisms involved have not yet been characterized. Here, we show that this protein is not only present in mammals but is widely distributed throughout eukaryotes both in its somatic and testicular forms. The secondary structure of the human somatic version consists mainly of clusters of alpha-helices and exists as a homodimer in solution. The protein binds nonspecifically to core histone H2A-H2B dimers and H3- ...[more]

PMID: 18456819

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