Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1998-12-24
pubmed:abstractText
The yeast Saccharomyces cerevisiae contains two related chromatin-remodeling complexes, RSC and SWI/SNF, which are shown to share the actin-related proteins Arp7 and Arp9. Depending on the genetic background tested, arp7 delta and arp9 delta mutants are either inviable or show greatly impaired growth and Swi-/Snf- mutant phenotypes. Unlike swi/snf mutants, viable arp7 delta or arp9 delta mutants have an Spt- phenotype, suggesting that RSC affects transcription. Temperature-sensitive mutations in ARP7 and ARP9 were isolated, and the amino acid changes support the structural relationship of Arp7 and Arp9 to actin. However, site-directed mutations predicted to impair ATP binding or hydrolysis did not detectably affect Arp7 or Arp9 function. Our results suggest that actin-related proteins perform important roles in chromatin-remodeling complexes by virtue of structural rather than enzymatic similarities to actin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Actins, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Chromatin, http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSC70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RSC complex, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SWI1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
639-51
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9844636-Actins, pubmed-meshheading:9844636-Adenosine Triphosphatases, pubmed-meshheading:9844636-Adenosine Triphosphate, pubmed-meshheading:9844636-Amino Acid Sequence, pubmed-meshheading:9844636-Amino Acid Substitution, pubmed-meshheading:9844636-Carrier Proteins, pubmed-meshheading:9844636-Cell Division, pubmed-meshheading:9844636-Chromatin, pubmed-meshheading:9844636-Chromosomal Proteins, Non-Histone, pubmed-meshheading:9844636-Conserved Sequence, pubmed-meshheading:9844636-DNA-Binding Proteins, pubmed-meshheading:9844636-Fungal Proteins, pubmed-meshheading:9844636-HSC70 Heat-Shock Proteins, pubmed-meshheading:9844636-HSP70 Heat-Shock Proteins, pubmed-meshheading:9844636-Molecular Sequence Data, pubmed-meshheading:9844636-Mutagenesis, Site-Directed, pubmed-meshheading:9844636-Phenotype, pubmed-meshheading:9844636-Protein Binding, pubmed-meshheading:9844636-Protein Structure, Secondary, pubmed-meshheading:9844636-Recombinant Fusion Proteins, pubmed-meshheading:9844636-Saccharomyces cerevisiae, pubmed-meshheading:9844636-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9844636-Transcription, Genetic, pubmed-meshheading:9844636-Transcription Factors
pubmed:year
1998
pubmed:articleTitle
Two actin-related proteins are shared functional components of the chromatin-remodeling complexes RSC and SWI/SNF.
pubmed:affiliation
Department of Structural Biology, Stanford University School of Medicine, California 94305, USA. bcairns@hci.utah.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't