(Q46676403)

24 December 2017

title

Site specificity of yeast histone acetyltransferase B complex in vivo (English)

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24 December 2017

author name string

Ana Poveda

series ordinal

1

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24 December 2017

Ramon Sendra

series ordinal

2

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24 December 2017

language of work or name

English

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publication date

28 March 2008

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24 December 2017

published in

FEBS Journal

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24 December 2017

volume

275

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24 December 2017

issue

9

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24 December 2017

page(s)

2122-2136

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24 December 2017

Functions of site-specific histone acetylation and deacetylation

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Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase

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Hif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus.

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Association with the origin recognition complex suggests a novel role for histone acetyltransferase Hat1p/Hat2p

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Type B histone acetyltransferase Hat1p participates in telomeric silencing

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Histone H3 and the histone acetyltransferase Hat1p contribute to DNA double-strand break repair

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Recruitment of the type B histone acetyltransferase Hat1p to chromatin is linked to DNA double-strand breaks

21 January 2018

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21 January 2018

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Histone acetyltransferase 1 is dispensable for replication-coupled chromatin assembly but contributes to recover DNA damages created following replication blockage in vertebrate cells

21 January 2018

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21 January 2018

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21 January 2018

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Evidence for eviction and rapid deposition of histones upon transcriptional elongation by RNA polymerase II.

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Hat1: the emerging cellular roles of a type B histone acetyltransferase

21 January 2018

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Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae

21 January 2018

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Epitope tagging of yeast genes using a PCR-based strategy: more tags and improved practical routines

21 January 2018

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Rapid and reliable protein extraction from yeast

21 January 2018

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Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines

21 January 2018

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10.1111/J.1742-4658.2008.06367.X

21 January 2018

Identifiers

DOI

1 reference

24 December 2017

PubMed ID

18373695

1 reference

24 December 2017