Linked Life Data

6360379

Source:http://linkedlifedata.com/resource/pubmed/id/6360379

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3 Pt 2
pubmed:dateCreated
1984-2-15
pubmed:databankReference
pubmed:abstractText
The basic amino terminus of each histone is external to the nucleosome core particle. In vitro studies have shown that the amino termini are not required for nucleosome assembly. To address the significance of these results in vivo we constructed mutations in yeast histone H2B in genetic backgrounds lacking wild-type H2B protein. We found that the protein can function in vivo even with large deletions at its amino terminus. These mutations produce no obvious phenotype and there appears to be no selection against the mutant proteins in chromatin assembly. A deletion removing a large portion of the carboxyl terminus was lethal. We conclude that much of the amino terminus of histone H2B has no essential function in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
711-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Yeast histone H2B containing large amino terminus deletions can function in vivo.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.