Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-7-20
pubmed:databankReference
pubmed:abstractText
In mammals, yeast and Drosophila, the histone deacetylase RPD3 proteins can alter the expression of genes involved in fundamental biological processes by affecting the degree of acetylation of histones and changing chromatin structure. Here we report the isolation of a cDNA sequence encoding an RPD3 homologue from maize, which is able to complement the phenotype of an rpd3 null mutant of the yeast Saccharomyces cerevisiae. The expression of the corresponding gene(s) was assessed in different maize tissues. The number of homologous loci was estimated by Southern hybridisation to be in the range of two to three, and the chromosomal location of one of these loci was determined. Phylogenetic analysis and tests for relative divergence rates, using related RPD3 sequences from different species, were performed, and suggest that different polymorphic forms of RPD3-like proteins that evolve at distinct rates are present in the species considered.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylase 1, http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases, http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RPD3 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Rpd3 protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0026-8925
pubmed:author
pubmed:issnType
Print
pubmed:volume
258
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
288-96
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9645435-Cloning, Molecular, pubmed-meshheading:9645435-Drosophila Proteins, pubmed-meshheading:9645435-Fungal Proteins, pubmed-meshheading:9645435-Genes, Reporter, pubmed-meshheading:9645435-Genetic Complementation Test, pubmed-meshheading:9645435-Histone Deacetylase 1, pubmed-meshheading:9645435-Histone Deacetylases, pubmed-meshheading:9645435-Mutation, pubmed-meshheading:9645435-Phylogeny, pubmed-meshheading:9645435-Plant Proteins, pubmed-meshheading:9645435-RNA, Messenger, pubmed-meshheading:9645435-Repressor Proteins, pubmed-meshheading:9645435-Saccharomyces cerevisiae, pubmed-meshheading:9645435-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9645435-Sequence Alignment, pubmed-meshheading:9645435-Sequence Analysis, DNA, pubmed-meshheading:9645435-Transcription Factors, pubmed-meshheading:9645435-Zea mays
pubmed:year
1998
pubmed:articleTitle
Identification and characterisation of an RPD3 homologue from maize (Zea mays L.) that is able to complement an rpd3 null mutant of Saccharomyces cerevisiae.
pubmed:affiliation
Istituto Sperimentale per la Ceralicoltura, Sezione di Bergamo, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't