A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme (Q27936754)

PubMed

PubMed publication ID

10445034

1 December 2016

title

A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme (English)

1 reference

PubMed

PubMed publication ID

10445034

Elongator subunit ELP3 YPL086C

1 December 2016

main subject

1 reference

GOA release 2020-03-11

author

Hediye Erdjument-Bromage

5

object named as

H Erdjument-Bromage

0 references

Charles David Allis

8

object named as

C D Allis

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author name string

B O Wittschieben

1

0 references

G Otero

2

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T de Bizemont

3

0 references

J Fellows

4

0 references

R Ohba

6

0 references

Y Li

7

0 references

P Tempst

9

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J Q Svejstrup

10

0 references

publication date

July 1999

0 references

language of work or name

0 references

1 reference

PubMed publication ID

10445034

An activity gel assay detects a single, catalytically active histone acetyltransferase subunit in Tetrahymena macronuclei

1 December 2016

volume

4

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issue

1

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page(s)

123-8

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cites work

1 reference

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Special HATs for special occasions: linking histone acetylation to chromatin assembly and gene activation

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Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation

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A Human RNA Polymerase II Complex Containing Factors That Modify Chromatin Structure

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Histone modifications in the yeast S. Cerevisiae

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Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily

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

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Examination of micro-tip reversed-phase liquid chromatographic extraction of peptide pools for mass spectrometric analysis

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6-Azauracil inhibition of GTP biosynthesis in Saccharomyces cerevisiae

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Nucleosome loss activates yeast downstream promoters in vivo

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Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae

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Core histone hyperacetylation co-maps with generalized DNase I sensitivity in the chicken beta-globin chromosomal domain.

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

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Dissecting the regulatory circuitry of a eukaryotic genome

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Transcription on nucleosomal templates by RNA polymerase II in vitro: inhibition of elongation with enhancement of sequence-specific pausing

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Effects of histone H4 depletion on the cell cycle and transcription of Saccharomyces cerevisiae

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Roles of histone acetyltransferases and deacetylases in gene regulation

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Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo

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Crystal structure of the nucleosome core particle at 2.8 Å resolution

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Methodical analysis of protein-nitrocellulose interactions to design a refined digestion protocol

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Use of mass spectrometric molecular weight information to identify proteins in sequence databases

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Linking histone acetylation to transcriptional regulation

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Change in the pattern of histone binding to DNA upon transcriptional activation

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FACT, a Factor that Facilitates Transcript Elongation through Nucleosomes

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Elongator, a Multisubunit Component of a Novel RNA Polymerase II Holoenzyme for Transcriptional Elongation

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The Biochemical and Phenotypic Characterization of Hho1p, the Putative Linker Histone H1 of Saccharomyces cerevisiae

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The RNA polymerase II general elongation factors

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The role of general initiation factors in transcription by RNA polymerase II

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Linker histone H1 regulates specific gene expression but not global transcription in vivo

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Linker histones are not essential and affect chromatin condensation in vivo

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The reprogramming of transcriptional competence

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Disruption of Higher-Order Folding by Core Histone Acetylation Dramatically Enhances Transcription of Nucleosomal Arrays by RNA Polymerase III

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DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs

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Histone Acetylation Is Required to Maintain the Unfolded Nucleosome Structure Associated with Transcribing DNA

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