No Cover Image

Journal article 79 views

Alteration of GCN5 levels in maize reveals dynamic responses to manipulating histone acetylation

Riyaz A. Bhat, Marcus Riehl, Geraldina Santandrea, Riccardo Velasco, Steve Slocombe, Günter Donn, Hans‐Henning Steinbiss, Richard D. Thompson, Heinz‐Albert Becker

The Plant Journal, Volume: 33, Issue: 3, Pages: 455 - 469

Swansea University Author: Steve Slocombe

Full text not available from this repository: check for access using links below.

Abstract

The role played by histone acetyltransferase (HAT), GCN5, in transcriptional co-activation has been analysed in detail in yeast and mammals. Here, we present the cloning and expression pattern of Zmgcn5, the maize homologue. The enzymatic activity of the recombinant ZmGCN5 was analysed with histone...

Full description

Published in: The Plant Journal
ISSN: 0960-7412 1365-313X
Published: Wiley 2003
Online Access: Check full text

URI: https://cronfa.swan.ac.uk/Record/cronfa65491
Tags: Add Tag
No Tags, Be the first to tag this record!
first_indexed 2024-01-22T14:46:50Z
last_indexed 2024-01-22T14:46:50Z
id cronfa65491
recordtype SURis
fullrecord <?xml version="1.0" encoding="utf-8"?><rfc1807 xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:xsd="http://www.w3.org/2001/XMLSchema"><bib-version>v2</bib-version><id>65491</id><entry>2024-01-22</entry><title>Alteration of GCN5 levels in maize reveals dynamic responses to manipulating histone acetylation</title><swanseaauthors><author><sid>4a1ea486a78ed357efdfa053a277ae40</sid><firstname>Steve</firstname><surname>Slocombe</surname><name>Steve Slocombe</name><active>true</active><ethesisStudent>false</ethesisStudent></author></swanseaauthors><date>2024-01-22</date><deptcode>SBI</deptcode><abstract>The role played by histone acetyltransferase (HAT), GCN5, in transcriptional co-activation has been analysed in detail in yeast and mammals. Here, we present the cloning and expression pattern of Zmgcn5, the maize homologue. The enzymatic activity of the recombinant ZmGCN5 was analysed with histone and nucleosome substrates. In situ hybridisation of developing maize kernels using Zmgcn5 as probe shows that the transcript is concentrated in rapidly dividing cells. To investigate the role of ZmGCN5 in the transcription of specific plant genes, direct protein-protein interactions were tested. A cDNA clone encoding a putative interacting partner in GCN5-adapter complexes, ZmADA2, was isolated and the interaction between ZmGCN5 and ZmADA2 was confirmed by a GST-spin down experiment. Co-immunoprecipitation of the plant transcriptional activator Opaque-2 and ZmADA2 in nuclear extracts suggests ADA2/GCN5-containing complexes to mediate transcriptional activation by binding of this bZIP factor. For a more general analysis of the effects of histone acetylation on plant gene expression, 2500 ESTs spotted on filters were hybridised with cDNA probes derived either from maize cell lines treated with Trichostatin A (TSA), or from a transgenic line expressing the ZmGCN5 antisense transcript. Several sequences showing marked changes in abundance were confirmed by RNA blot analysis. Inhibition of histone deacetylation with TSA is accompanied by a decrease in the abundance of ZmGCN5 acetylase protein, but by increases in mRNAs for histones H2A, H2B, H3 and H4. The elevated histone mRNA levels were not reflected in increasing histone protein concentrations, suggesting hyperacetylated histones arising from TSA treatment may be preferentially degraded and substituted by de novo synthesised histones. The ZmGCN5 antisense material showed suppression of the endogenous ZmGCN5 transcript and the profiling analysis revealed increased mRNA levels for H2A, H2B and H4. Furthermore, in the antisense line, a reduction in the amount of the RPD3-type HD1B-I histone deacetylase protein was observed. A model for linked regulation of histone acetylation and histone mRNA transcription is discussed.</abstract><type>Journal Article</type><journal>The Plant Journal</journal><volume>33</volume><journalNumber>3</journalNumber><paginationStart>455</paginationStart><paginationEnd>469</paginationEnd><publisher>Wiley</publisher><placeOfPublication/><isbnPrint/><isbnElectronic/><issnPrint>0960-7412</issnPrint><issnElectronic>1365-313X</issnElectronic><keywords>histone acetyltransferase, co-activator, GCN5, ADA2, maize, Tricnostatin A</keywords><publishedDay>6</publishedDay><publishedMonth>2</publishedMonth><publishedYear>2003</publishedYear><publishedDate>2003-02-06</publishedDate><doi>10.1046/j.1365-313x.2003.01642.x</doi><url/><notes/><college>COLLEGE NANME</college><department>Biosciences</department><CollegeCode>COLLEGE CODE</CollegeCode><DepartmentCode>SBI</DepartmentCode><institution>Swansea University</institution><apcterm/><funders/><projectreference/><lastEdited>2024-03-21T16:13:21.8394555</lastEdited><Created>2024-01-22T14:45:57.4560734</Created><path><level id="1">Faculty of Science and Engineering</level><level id="2">School of Biosciences, Geography and Physics - Biosciences</level></path><authors><author><firstname>Riyaz A.</firstname><surname>Bhat</surname><order>1</order></author><author><firstname>Marcus</firstname><surname>Riehl</surname><order>2</order></author><author><firstname>Geraldina</firstname><surname>Santandrea</surname><order>3</order></author><author><firstname>Riccardo</firstname><surname>Velasco</surname><order>4</order></author><author><firstname>Steve</firstname><surname>Slocombe</surname><order>5</order></author><author><firstname>Günter</firstname><surname>Donn</surname><order>6</order></author><author><firstname>Hans‐Henning</firstname><surname>Steinbiss</surname><order>7</order></author><author><firstname>Richard D.</firstname><surname>Thompson</surname><order>8</order></author><author><firstname>Heinz‐Albert</firstname><surname>Becker</surname><order>9</order></author></authors><documents/><OutputDurs/></rfc1807>
spelling v2 65491 2024-01-22 Alteration of GCN5 levels in maize reveals dynamic responses to manipulating histone acetylation 4a1ea486a78ed357efdfa053a277ae40 Steve Slocombe Steve Slocombe true false 2024-01-22 SBI The role played by histone acetyltransferase (HAT), GCN5, in transcriptional co-activation has been analysed in detail in yeast and mammals. Here, we present the cloning and expression pattern of Zmgcn5, the maize homologue. The enzymatic activity of the recombinant ZmGCN5 was analysed with histone and nucleosome substrates. In situ hybridisation of developing maize kernels using Zmgcn5 as probe shows that the transcript is concentrated in rapidly dividing cells. To investigate the role of ZmGCN5 in the transcription of specific plant genes, direct protein-protein interactions were tested. A cDNA clone encoding a putative interacting partner in GCN5-adapter complexes, ZmADA2, was isolated and the interaction between ZmGCN5 and ZmADA2 was confirmed by a GST-spin down experiment. Co-immunoprecipitation of the plant transcriptional activator Opaque-2 and ZmADA2 in nuclear extracts suggests ADA2/GCN5-containing complexes to mediate transcriptional activation by binding of this bZIP factor. For a more general analysis of the effects of histone acetylation on plant gene expression, 2500 ESTs spotted on filters were hybridised with cDNA probes derived either from maize cell lines treated with Trichostatin A (TSA), or from a transgenic line expressing the ZmGCN5 antisense transcript. Several sequences showing marked changes in abundance were confirmed by RNA blot analysis. Inhibition of histone deacetylation with TSA is accompanied by a decrease in the abundance of ZmGCN5 acetylase protein, but by increases in mRNAs for histones H2A, H2B, H3 and H4. The elevated histone mRNA levels were not reflected in increasing histone protein concentrations, suggesting hyperacetylated histones arising from TSA treatment may be preferentially degraded and substituted by de novo synthesised histones. The ZmGCN5 antisense material showed suppression of the endogenous ZmGCN5 transcript and the profiling analysis revealed increased mRNA levels for H2A, H2B and H4. Furthermore, in the antisense line, a reduction in the amount of the RPD3-type HD1B-I histone deacetylase protein was observed. A model for linked regulation of histone acetylation and histone mRNA transcription is discussed. Journal Article The Plant Journal 33 3 455 469 Wiley 0960-7412 1365-313X histone acetyltransferase, co-activator, GCN5, ADA2, maize, Tricnostatin A 6 2 2003 2003-02-06 10.1046/j.1365-313x.2003.01642.x COLLEGE NANME Biosciences COLLEGE CODE SBI Swansea University 2024-03-21T16:13:21.8394555 2024-01-22T14:45:57.4560734 Faculty of Science and Engineering School of Biosciences, Geography and Physics - Biosciences Riyaz A. Bhat 1 Marcus Riehl 2 Geraldina Santandrea 3 Riccardo Velasco 4 Steve Slocombe 5 Günter Donn 6 Hans‐Henning Steinbiss 7 Richard D. Thompson 8 Heinz‐Albert Becker 9
title Alteration of GCN5 levels in maize reveals dynamic responses to manipulating histone acetylation
spellingShingle Alteration of GCN5 levels in maize reveals dynamic responses to manipulating histone acetylation
Steve Slocombe
title_short Alteration of GCN5 levels in maize reveals dynamic responses to manipulating histone acetylation
title_full Alteration of GCN5 levels in maize reveals dynamic responses to manipulating histone acetylation
title_fullStr Alteration of GCN5 levels in maize reveals dynamic responses to manipulating histone acetylation
title_full_unstemmed Alteration of GCN5 levels in maize reveals dynamic responses to manipulating histone acetylation
title_sort Alteration of GCN5 levels in maize reveals dynamic responses to manipulating histone acetylation
author_id_str_mv 4a1ea486a78ed357efdfa053a277ae40
author_id_fullname_str_mv 4a1ea486a78ed357efdfa053a277ae40_***_Steve Slocombe
author Steve Slocombe
author2 Riyaz A. Bhat
Marcus Riehl
Geraldina Santandrea
Riccardo Velasco
Steve Slocombe
Günter Donn
Hans‐Henning Steinbiss
Richard D. Thompson
Heinz‐Albert Becker
format Journal article
container_title The Plant Journal
container_volume 33
container_issue 3
container_start_page 455
publishDate 2003
institution Swansea University
issn 0960-7412
1365-313X
doi_str_mv 10.1046/j.1365-313x.2003.01642.x
publisher Wiley
college_str Faculty of Science and Engineering
hierarchytype
hierarchy_top_id facultyofscienceandengineering
hierarchy_top_title Faculty of Science and Engineering
hierarchy_parent_id facultyofscienceandengineering
hierarchy_parent_title Faculty of Science and Engineering
department_str School of Biosciences, Geography and Physics - Biosciences{{{_:::_}}}Faculty of Science and Engineering{{{_:::_}}}School of Biosciences, Geography and Physics - Biosciences
document_store_str 0
active_str 0
description The role played by histone acetyltransferase (HAT), GCN5, in transcriptional co-activation has been analysed in detail in yeast and mammals. Here, we present the cloning and expression pattern of Zmgcn5, the maize homologue. The enzymatic activity of the recombinant ZmGCN5 was analysed with histone and nucleosome substrates. In situ hybridisation of developing maize kernels using Zmgcn5 as probe shows that the transcript is concentrated in rapidly dividing cells. To investigate the role of ZmGCN5 in the transcription of specific plant genes, direct protein-protein interactions were tested. A cDNA clone encoding a putative interacting partner in GCN5-adapter complexes, ZmADA2, was isolated and the interaction between ZmGCN5 and ZmADA2 was confirmed by a GST-spin down experiment. Co-immunoprecipitation of the plant transcriptional activator Opaque-2 and ZmADA2 in nuclear extracts suggests ADA2/GCN5-containing complexes to mediate transcriptional activation by binding of this bZIP factor. For a more general analysis of the effects of histone acetylation on plant gene expression, 2500 ESTs spotted on filters were hybridised with cDNA probes derived either from maize cell lines treated with Trichostatin A (TSA), or from a transgenic line expressing the ZmGCN5 antisense transcript. Several sequences showing marked changes in abundance were confirmed by RNA blot analysis. Inhibition of histone deacetylation with TSA is accompanied by a decrease in the abundance of ZmGCN5 acetylase protein, but by increases in mRNAs for histones H2A, H2B, H3 and H4. The elevated histone mRNA levels were not reflected in increasing histone protein concentrations, suggesting hyperacetylated histones arising from TSA treatment may be preferentially degraded and substituted by de novo synthesised histones. The ZmGCN5 antisense material showed suppression of the endogenous ZmGCN5 transcript and the profiling analysis revealed increased mRNA levels for H2A, H2B and H4. Furthermore, in the antisense line, a reduction in the amount of the RPD3-type HD1B-I histone deacetylase protein was observed. A model for linked regulation of histone acetylation and histone mRNA transcription is discussed.
published_date 2003-02-06T16:13:22Z
_version_ 1794152964904976384
score 11.013148