Phosphorylation of linker histone H1 regulates gene expression in vivo by mimicking H1 removal

Yali Dou; Craig A. Mizzen; Marc Abrams; C. David Allis; Martin A. Gorovsky

doi:10.1016/S1097-2765(00)80215-4

Phosphorylation of linker histone H1 regulates gene expression in vivo by mimicking H1 removal

Yali Dou, Craig A. Mizzen, Marc Abrams, C. David Allis, Martin A. Gorovsky

Research output: Contribution to journal › Article › peer-review

Abstract

Two Tetrahymena strains were created by gene replacement. One contained H1 with all phosphorylation sites mutated to alanine, preventing phosphorylation. The other had these sites changed to glutamic acid, mimicking the fully phosphorylated state. Global gene expression was not detectably changed in either strain. Instead, H1 phosphorylation activated or repressed specific genes in a manner that was remarkably similar to the effects of knocking out the gene encoding H1. These studies demonstrate a role for H1 phosphorylation in the regulation of transcription in vivo and suggest that it acts by mimicking the partial removal of H1.

Original language	English (US)
Pages (from-to)	641-647
Number of pages	7
Journal	Molecular cell
Volume	4
Issue number	4
DOIs	https://doi.org/10.1016/S1097-2765(00)80215-4
State	Published - Oct 1999
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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title = "Phosphorylation of linker histone H1 regulates gene expression in vivo by mimicking H1 removal",

abstract = "Two Tetrahymena strains were created by gene replacement. One contained H1 with all phosphorylation sites mutated to alanine, preventing phosphorylation. The other had these sites changed to glutamic acid, mimicking the fully phosphorylated state. Global gene expression was not detectably changed in either strain. Instead, H1 phosphorylation activated or repressed specific genes in a manner that was remarkably similar to the effects of knocking out the gene encoding H1. These studies demonstrate a role for H1 phosphorylation in the regulation of transcription in vivo and suggest that it acts by mimicking the partial removal of H1.",

author = "Yali Dou and Mizzen, {Craig A.} and Marc Abrams and Allis, {C. David} and Gorovsky, {Martin A.}",

note = "Funding Information: This work was supported by grants from the NIH to M. A. G. (GM21793) and C. D. A. (GM40922).",

year = "1999",

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doi = "10.1016/S1097-2765(00)80215-4",

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T1 - Phosphorylation of linker histone H1 regulates gene expression in vivo by mimicking H1 removal

AU - Dou, Yali

AU - Mizzen, Craig A.

AU - Abrams, Marc

AU - Allis, C. David

AU - Gorovsky, Martin A.

N1 - Funding Information: This work was supported by grants from the NIH to M. A. G. (GM21793) and C. D. A. (GM40922).

PY - 1999/10

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N2 - Two Tetrahymena strains were created by gene replacement. One contained H1 with all phosphorylation sites mutated to alanine, preventing phosphorylation. The other had these sites changed to glutamic acid, mimicking the fully phosphorylated state. Global gene expression was not detectably changed in either strain. Instead, H1 phosphorylation activated or repressed specific genes in a manner that was remarkably similar to the effects of knocking out the gene encoding H1. These studies demonstrate a role for H1 phosphorylation in the regulation of transcription in vivo and suggest that it acts by mimicking the partial removal of H1.

AB - Two Tetrahymena strains were created by gene replacement. One contained H1 with all phosphorylation sites mutated to alanine, preventing phosphorylation. The other had these sites changed to glutamic acid, mimicking the fully phosphorylated state. Global gene expression was not detectably changed in either strain. Instead, H1 phosphorylation activated or repressed specific genes in a manner that was remarkably similar to the effects of knocking out the gene encoding H1. These studies demonstrate a role for H1 phosphorylation in the regulation of transcription in vivo and suggest that it acts by mimicking the partial removal of H1.

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Phosphorylation of linker histone H1 regulates gene expression in vivo by mimicking H1 removal

Abstract

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