Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2000-2-1
pubmed:abstractText
Despite its conservation in organisms from bacteria to human and its general requirement for transcriptional silencing in yeast, the function of the Sir2 protein is unknown. Here we show that Sir2 can transfer labeled phosphate from nicotinamide adenine dinucleotide to itself and histones in vitro. A modified form of Sir2, which results from its automodification activity, is specifically recognized by anti-mono-ADP-ribose antibodies, suggesting that Sir2 is an ADP-ribosyltransferase. Mutation of a phylogenetically invariant histidine residue in Sir2 abolishes both its enzymatic activity in vitro and its silencing functions in vivo. However, the mutant protein is associated with chromatin and other silencing factors in a manner similar to wild-type Sir2. These findings suggest that Sir2 contains an ADP-ribosyltransferase activity that is essential for its silencing function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Ribosomal, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases, http://linkedlifedata.com/resource/pubmed/chemical/Histones, http://linkedlifedata.com/resource/pubmed/chemical/NAD, http://linkedlifedata.com/resource/pubmed/chemical/Poly(ADP-ribose) Polymerases, http://linkedlifedata.com/resource/pubmed/chemical/SIR2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/SIRT1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Silent Information Regulator..., http://linkedlifedata.com/resource/pubmed/chemical/Sirtuin 1, http://linkedlifedata.com/resource/pubmed/chemical/Sirtuin 2, http://linkedlifedata.com/resource/pubmed/chemical/Sirtuins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
735-45
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10619427-Amino Acid Sequence, pubmed-meshheading:10619427-Blotting, Western, pubmed-meshheading:10619427-Chromatin, pubmed-meshheading:10619427-DNA, Ribosomal, pubmed-meshheading:10619427-DNA-Binding Proteins, pubmed-meshheading:10619427-Fungal Proteins, pubmed-meshheading:10619427-Gene Silencing, pubmed-meshheading:10619427-Genes, Fungal, pubmed-meshheading:10619427-Histone Deacetylases, pubmed-meshheading:10619427-Histones, pubmed-meshheading:10619427-Molecular Sequence Data, pubmed-meshheading:10619427-NAD, pubmed-meshheading:10619427-Poly(ADP-ribose) Polymerases, pubmed-meshheading:10619427-Precipitin Tests, pubmed-meshheading:10619427-Silent Information Regulator Proteins, Saccharomyces..., pubmed-meshheading:10619427-Sirtuin 1, pubmed-meshheading:10619427-Sirtuin 2, pubmed-meshheading:10619427-Sirtuins, pubmed-meshheading:10619427-Telomere, pubmed-meshheading:10619427-Trans-Activators, pubmed-meshheading:10619427-Yeasts
pubmed:year
1999
pubmed:articleTitle
An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing.
pubmed:affiliation
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't