Linked Life Data

17623908

Source:http://linkedlifedata.com/resource/pubmed/id/17623908

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2007-7-12
pubmed:abstractText
Alterations in the chromatin structure are essential for easy accesses to chromosomal DNA. Such architectural alterations can be achieved by four means: (i) variants of histone subtypes, (ii) chromatin remodeling, (iii) post-translational modification, and (iv) chromatin assembly. This chapter discusses mainly on the first, third and fourth mechanisms, and especially on the acetylation of core histones, one of the third mechanisms. Taking the advantage of the gene targeting technique, we systematically established numerous mutant DT40 cell lines, each lacking particular gene, of interest such that encoding histones, histone deacetylases (HDACs), acetyltransferases (HATs) and chaperones, etc. Every subtype member of the histone gene family is capable of compensating the loss of others to maintain the mRNA level of each histone subtype, and most of histone variants are involved positively or negatively in the transcription regulation of particular genes. Regarding HDACs, HDAC-2 controls the amount of the IgM H-chain at the steps of both transcription and alternative pre-mRNA processing, and HDAC-3 is indispensable for cell viability. Concerning HATs, GCN5 has tremendous impact on growth kinetics by preferentially acting as a supervisor in the normal cell cycle progression. The distinct participatory roles of the N-terminal and C-terminal halves of HIRA, one of histone chaperones, in both cell growth and transcription regulations of cell cycle-related genes, have also been highlighted. Therefore, the gene targeting technique in the DT40 cell line can be used as a powerful tool for the functional analysis of histones, histone modifying enzymes and histone chaperones relevant to chromatin biology.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0306-0225
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
225-43
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Participation of histones, histone modifying enzymes and histone chaperones in vertebrate cell functions.
pubmed:affiliation
Department of Life Science, Frontier Science Research Center, Miyazaki Medical College, University of Miyazaki, 5200, Kihara, Kiyotake, Miyazaki 889-1692, Japan.
pubmed:publicationType
Journal Article, Review