Literature DB >> 1412698

Chromatin condensation: does histone H1 dephosphorylation play a role?

S Y Roth1, C D Allis.   

Abstract

In this article we describe three distinct biological systems where histone H1 phosphorylation is uncoupled from mitosis and highly condensed chromatin is enriched in dephosphorylated forms of H1: the amitotic macronucleus of Tetrahymena, terminally differentiated avian erythrocytes and sea urchin sperm. Each system offers informative contrasts to the idea that H1 hyperphosphorylation is causally related to mitotic chromosome condensation. Assuming that higher order chromatin folding is primarily driven by electrostatic interactions between H1 and DNA, an alternative model is presented for the role of H1 phosphorylation in chromatin condensation.

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Year:  1992        PMID： 1412698     DOI： 10.1016/0968-0004(92)90243-3

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN： 0968-0004            Impact factor:   13.807


  70 in total

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Review 7.  Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length.

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