(Q43803659)

27 November 2017

Acetylation of the yeast histone H4 N terminus regulates its binding to heterochromatin protein SIR3. (English)

1 reference

27 November 2017

3

Michael Grunstein

1 reference

27 November 2017

Andrew A Carmen

1

1 reference

PubMed ID

11714726

27 November 2017

Lisa Milne

series ordinal

2

1 reference

PubMed ID

11714726

27 November 2017

language of work or name

English

0 references

publication date

19 November 2001

1 reference

Journal of Biological Chemistry

27 November 2017

1 reference

27 November 2017

277

1 reference

27 November 2017

4778-4781

1 reference

27 November 2017

7

1 reference

Histones and the regulation of heterochromatin in yeast.

27 November 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Evidence that a complex of SIR proteins interacts with the silencer and telomere-binding protein RAP1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: a molecular model for the formation of heterochromatin in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Histone H3 amino terminus is required for telomeric and silent mating locus repression in yeast.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Spreading of transcriptional repressor SIR3 from telomeric heterochromatin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Telomere folding is required for the stable maintenance of telomere position effects in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Telomere-proximal DNA in Saccharomyces cerevisiae is refractory to methyltransferase activity in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Genomewide studies of histone deacetylase function in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Point mutations in the yeast histone H4 gene prevent silencing of the silent mating type locus HML.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Structure and function of a human TAFII250 double bromodomain module

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Redistribution of silencing proteins from telomeres to the nucleolus is associated with extension of life span in S. cerevisiae.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Silent domains are assembled continuously from the telomere and are defined by promoter distance and strength, and by SIR3 dosage

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Modulation of chromatin folding by histone acetylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Effects of histone acetylation on the solubility and folding of the chromatin fiber

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

Acetylation increases the alpha-helical content of the histone tails of the nucleosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110532200

21 January 2018

Identifiers

DOI

10.1074/JBC.M110532200

1 reference

27 November 2017

1 reference

PubMed ID

11714726