Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1998-5-1
pubmed:abstractText
Posttranslational acetylation of core histone amino termini has long been associated with transcriptionally active chromatin. Recent reports have demonstrated histone acetyltransferase activity in a small group of conserved transcriptional regulators directly linked to gene activation. In addition, the presence of a putative acetyltransferase domain has been discovered in a group of proteins known as the MYST family (for its founding members MOZ, YBF2/SAS3, SAS2, and Tip60). Members of this family are implicated in acute myeloid leukemia (MOZ), transcriptional silencing in yeast (SAS2 and YBF2/SAS3), HIV Tat interaction in humans (Tip60), and dosage compensation in Drosophila (MOF). In this report, we express a yeast ORF with homology to MYST family members and show it possesses histone acetyltransferase activity. Unlike the other MYST family members in Saccharomyces cerevisiae this gene is essential for growth.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-14172992, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-1568251, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-2044150, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-2106160, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-2249688, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-2551674, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-3080415, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-7217105, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-7559580, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-7603997, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-7747518, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-7762301, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-7862667, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8034606, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8288132, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8601308, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8607265, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8702554, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8722174, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8754835, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8782817, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8782818, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8805705, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8858142, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8858151, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-8980232, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-9077451, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-9081669, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-9093847, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-9155031, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-9175471, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-9224714, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-9296499, http://linkedlifedata.com/resource/pubmed/commentcorrection/9520405-9388189
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3561-5
pubmed:dateRevised
2011-10-27
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
ESA1 is a histone acetyltransferase that is essential for growth in yeast.
pubmed:affiliation
Department of Biology, University of Rochester, Rochester, NY 14627, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.