Phosphorylation of linker histone H1 regulates gene expression in vivo by mimicking H1 removal.
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.
Dou
Y
Y
Department of Biology, University of Rochester, New York 14627, USA.
Mizzen
C A
CA
Abrams
M
M
Allis
C D
CD
Gorovsky
M A
MA
D000818:Animals; D030801:Animals, Genetically Modified; D004268:DNA-Binding Proteins / Q000235:genetics; D005786:Gene Expression Regulation / Q000235:genetics*; D017125:Genes, Protozoan / Q000235:genetics; D006657:Histones / Q000235:genetics*; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D010766:Phosphorylation; D015800:Protozoan Proteins / Q000235:genetics; D012333:RNA, Messenger / Q000378:metabolism; D016808:Tetrahymena thermophila / Q000235:genetics*; D014170:Transformation, Genetic
D004268:DNA-Binding Proteins; D006657:Histones; D015800:Protozoan Proteins; D012333:RNA, Messenger