Linked Life Data

11430834

Source:http://linkedlifedata.com/resource/pubmed/id/11430834

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2001-6-29
pubmed:abstractText
Histone H2A.Z is structurally and functionally distinct from the major H2As. To understand the function of H2A.Z acetylation, we performed a mutagenic analysis of the six acetylated lysines in the N-terminal tail of Tetrahymena H2A.Z. Tetrahymena cannot survive with arginines at all six sites. Retention of one acetylatable lysine is sufficient to provide the essential function of H2A.Z acetylation. This essential function can be mimicked by deleting the region encompassing all six sites, or by mutations that reduce the positive charge of the N terminus at the acetylation sites themselves, or at other sites in the tail. These properties argue that the essential function of H2A.Z acetylation is to modify a "charge patch" by reducing the charge of the tail.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1329-35
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Histone H2A.Z acetylation modulates an essential charge patch.
pubmed:affiliation
Department of Biology, University of Rochester, 14627, Rochester, NY, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.