Yeast histone H4 N-terminal sequence is required for promoter activation in vivo

@article{Durrin1991YeastHH,
  title={Yeast histone H4 N-terminal sequence is required for promoter activation in vivo},
  author={Linda K. Durrin and Randall K Mann and Paul S. Kayne and Michael Grunstein},
  journal={Cell},
  year={1991},
  volume={65},
  pages={1023-1031}
}
Global and specific transcriptional repression by the histone H3 amino terminus in yeast
TLDR
Derepression in the absence of the H3 amino terminus requires the primary activator of this promoter, Cha4p, which is shown by chromatin immunoprecipitation to be constitutively bound to the CHA1 promoter in WT yeast.
Redundant Roles for Histone H3 N-Terminal Lysine Residues in Subtelomeric Gene Repression in Saccharomyces cerevisiae
TLDR
It is proposed that acetylation and methylation of histone H3 N-terminal lysine residues act as redundant mechanisms to demarcate regions of euchromatin from heterochromatin.
All four core histone N‐termini contain sequences required for the repression of basal transcription in yeast.
TLDR
This work has found for each histone that the N‐terminal sequences repressing basal activity are in a short region adjacent to the structured alpha‐helical core, providing a means by which basal factors may recognize otherwise repressed regulatory elements.
Solution structures of the N-terminal domain of histone H4.
TLDR
The results suggest that N-terminal acetylated region of H4 prefers an extended backbone conformation at neutral pH, however, upon acetylation, the regions containing lysine residues induce structural transition, having defined structural form for its optimum function.
Genome-Wide Analysis of the Relationship between Transcriptional Regulation by Rpd3p and the Histone H3 and H4 Amino Termini in Budding Yeast
TLDR
It is suggested that acetylation of either the H3 or the H4 amino terminus could suffice to allow the activation of such genes, and the relationship between H3 tails and H4 tails in global gene expression is examined to find substantial overlap among the gene sets regulated by these histone tails.
Functional analysis of histones H2A and H2B in transcriptional repression in Saccharomyces cerevisiae.
TLDR
Results suggest that repressive chromatin structure may be established through the interactions of the Spt proteins with these histones, and other proteins, the products of the HIR (histone regulation) genes, may function to direct H2A and H2B to specific promoters.
A new class of histone H2A mutations in Saccharomyces cerevisiae causes specific transcriptional defects in vivo
TLDR
A new class of mutations in the histone H2A-encoding gene HTA1 that causes transcriptional defects at the SNF/SWI-dependent gene SUC2 is identified that may identify an additional step that is required to overcome repression by chromatin.
Amino acid substitutions in the structured domains of histones H3 and H4 partially relieve the requirement of the yeast SWI/SNF complex for transcription.
TLDR
The ability of mutations affecting the structure of the histone octamer to relieve the need for SWI and SNF products supports the proposal that the SWI/SNF complex stimulates transcription by altering chromatin structure and can account for the apparent conservation of SWI or SNF proteins in eukaryotes other than yeast.
Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase
TLDR
It is found that in vivo, GCN5 is required either directly or indirectly for the acetylation of several sites in H3 and H4 in addition to those recognized by the recombinant enzyme in vitro.
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Cell undergoing nucleosome depletion synthesized large quantities of accurate PHO5 transcripts even under repressive, high inorganic phosphate conditions, suggesting that nucleosomes regulatePHO5 transcription.
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The structure-function relations of the amino-terminal domain of yeast histone H4 were examined by the creation of directed point mutations and provide genetic proof for the roles of the H4 amino- terminal domain lysines in gene expression, replication, and nuclear division.
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TLDR
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