UTL Repository >
ISA - Instituto Superior de Agronomia >
DBEB - Departamento de Botânica e Engenharia Biologica >
CBAA - Centro de Botânica aplicada à Agricultura >
CBAA - Artigos de Revista >

Please use this identifier to cite or link to this item: http://hdl.handle.net/10400.5/2848

Title: Phosphorilation of histone H3 in plants - a dynamic affair
Authors: Houben, Andreas
Demidov, Dmitri
Caperta, A.
Karimi, Raheleh
Agueci, Francesco
Vlasenko, Liudmila
Keywords: histone phosphorylation
chromosomes
centromeres
cell cycle
aurora kinases
Issue Date: 2007
Publisher: Elsevier
Citation: "Biochimica et Biophysica Acta". ISSN 0167-4781. 1769 (2007) 308-315
Abstract: Histones are the main protein components of chromatin: they undergo extensive post-translational modifications, particularly acetylation, methylation, phosphorylation, ubiquitination and ADP-ribosylation which modify the structural/functional properties of chromatin. Posttranslational modifications of the N-terminal tails of the core histones within the nucleosome particle are thought to act as signals from the chromatin to the cell, for various processes. Thus, in many ways histone tails can be viewed as complex protein–protein interaction surfaces that are regulated by numerous post-translational modifications. Histone phosphorylation has been linked to chromosome condensation/segregation, activation of transcription, apoptosis and DNA damage repair. In plants, the cell cycle dependent phosphorylation of histone H3 has been described; it is hyperphosphorylated at serines 10/28 and at threonines 3/11 during both mitosis and meiosis in patterns that are specifically coordinated in both space and time. Although this post-translational modification is highly conserved, data show that the chromosomal distribution of individual modifications can differ between groups of eukaryotes. Initial results indicate that members of the plant Aurora kinase family have the capacity to control cell cycle regulated histone H3 phosphorylation, and in addition we describe other potential H3 kinases and discuss their functions.
URI: http://hdl.handle.net/10400.5/2848
ISSN: 0167-4781
Publisher version: www.elsevier.com/locate/bbaexp
Appears in Collections:CBAA - Artigos de Revista

Files in This Item:

File Description SizeFormat
REP-5-2007 Houben et al. BBA Phosphorylation of histone H3 in plants—A dynamic affair.pdf1.04 MBAdobe PDFView/Open
Statistics
FacebookTwitterDeliciousLinkedInDiggGoogle BookmarksMySpaceOrkut
Formato BibTex mendeley Endnote Logotipo do DeGóis 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

 

 
Estamos no RCAAP Governo Português separator Ministério da Educação e Ciência   Fundação para a Ciência e a Tecnologia

Financiado por:

POS_C UE