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rdf:type |
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lifeskim:mentions |
umls-concept:C0292369,
umls-concept:C0542341,
umls-concept:C0812273,
umls-concept:C0936012,
umls-concept:C1334043,
umls-concept:C1514562,
umls-concept:C1704461,
umls-concept:C1705535,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2697616
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pubmed:issue |
2
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pubmed:dateCreated |
2005-9-16
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pubmed:abstractText |
Inactivation on both alleles of the hSNF5/INI1 tumor suppressor gene which encodes a subunit of the human SWI/SNF chromatin remodelling complex occurs in most malignant rhabdoid tumors. No paralog of hSNF5/INI1 is identified in the human genome. In contrast, it has two homologs in the yeast Saccharomyces cerevisiae, SNF5 and SFH1 which encode core components of the ySWI/SNF and RSC complexes, respectively. The homology mainly concerns an approximately 200 amino acid region termed the SNF5 homology domain. We have tested the ability of the hSNF5/INI1-wild type gene product and of chimerical constructs in which the yeast SNF5 domains were replaced by that of the human protein, to complement yeast snf5 and sfh1 phenotypes. Neither growth deficiencies on different carbon sources of snf5 yeasts nor the lethality of the sfh1 phenotype could be rescued. This strongly suggests that the SNF5 homology domain presents species-specific functions.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
336
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
634-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16154112-Amino Acid Sequence,
pubmed-meshheading:16154112-Amino Acid Substitution,
pubmed-meshheading:16154112-Binding Sites,
pubmed-meshheading:16154112-Cell Proliferation,
pubmed-meshheading:16154112-Cell Survival,
pubmed-meshheading:16154112-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:16154112-DNA-Binding Proteins,
pubmed-meshheading:16154112-Humans,
pubmed-meshheading:16154112-Molecular Sequence Data,
pubmed-meshheading:16154112-Mutagenesis, Site-Directed,
pubmed-meshheading:16154112-Protein Binding,
pubmed-meshheading:16154112-Protein Structure, Tertiary,
pubmed-meshheading:16154112-Recombinant Proteins,
pubmed-meshheading:16154112-Saccharomyces cerevisiae,
pubmed-meshheading:16154112-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:16154112-Sequence Homology, Amino Acid,
pubmed-meshheading:16154112-Species Specificity,
pubmed-meshheading:16154112-Structure-Activity Relationship,
pubmed-meshheading:16154112-Transcription Factors
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pubmed:year |
2005
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pubmed:articleTitle |
Complementation analyses suggest species-specific functions of the SNF5 homology domain.
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pubmed:affiliation |
INSERM U509, Laboratoire de Pathologie Moléculaire des Cancers, Institut Curie, 26 rue d'Ulm, 75248 Paris, Cedex 05, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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