Redundant roles for histone H3 N-terminal lysine residues in subtelomeric gene repression in Saccharomyces cerevisiae

Amy M Martin; Derek J Pouchnik; Jennifer L Walker; John J Wyrick

doi:10.1534/genetics.104.026674

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Redundant roles for histone H3 N-terminal lysine residues in subtelomeric gene repression in Saccharomyces cerevisiae

Journal article

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Redundant roles for histone H3 N-terminal lysine residues in subtelomeric gene repression in Saccharomyces cerevisiae

Amy M Martin, Derek J Pouchnik, Jennifer L Walker and John J Wyrick

Genetics (Austin), Vol.167(3), pp.1123-1132

07/2004

DOI: https://doi.org/10.1534/genetics.104.026674

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https://hdl.handle.net/2376/114214

PMCID: PMC1470950

PMID: 15280228

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Abstract

Amino Acid Sequence

Mutagenesis, Site-Directed

Species Specificity

Saccharomyces cerevisiae - genetics

Gene Silencing

Molecular Sequence Data

Gene Expression Profiling

Mutation - genetics

DNA Methylation

Histones - genetics

Heterochromatin - metabolism

Plasmids - genetics

Lysine - metabolism

Models, Genetic

Acetylation

Histones - metabolism

Telomere - genetics

The transcription of genes located in subtelomeric regions of yeast chromosomes is repressed relative to the rest of the genome. This repression requires wild-type nucleosome levels but not the telomere silencing factors Sir2, Sir3, Sir4, and Rap1. Subtelomeric heterochromatin is characterized by the absence of acetylation or methylation of histone H3 lysine residues, but it is not known whether histone H3 hypoacetylation or hypomethylation is a prerequisite for the establishment of subtelomeric heterochromatin. We have systematically mutated the N-terminal tails of histone H3 and H4 in Saccharomyces cerevisiae and characterized the effects each mutant has on genome-wide expression. Our results show that subtelomeric transcriptional repression is dependent on the histone H3 N-terminal domain, but not the histone H4 N-terminal domain. Mutating lysine-4, lysine-9, lysine-14, lysine-18, lysine-23, and lysine-27 to glycine in histone H3 is also sufficient to significantly reduce subtelomeric gene repression. Individual histone H3 lysine mutations, however, have little effect on subtelomeric gene repression or genome-wide expression, indicating that these six lysine residues have redundant functions. We propose that acetylation and methylation of histone H3 N-terminal lysine residues act as redundant mechanisms to demarcate regions of euchromatin from heterochromatin.

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Title: Redundant roles for histone H3 N-terminal lysine residues in subtelomeric gene repression in Saccharomyces cerevisiae
Creators: Amy M Martin - School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4660, USA
Derek J Pouchnik
Jennifer L Walker
John J Wyrick
Publication Details: Genetics (Austin), Vol.167(3), pp.1123-1132
Academic Unit: Molecular Biosciences, School of
Publisher: United States
Identifiers: 99900547658701842
Language: English
Resource Type: Journal article