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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-3
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pubmed:dateCreated |
2002-12-30
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pubmed:databankReference |
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pubmed:abstractText |
The two human proteins Ki-1/57 and CGI-55 have highly similar amino acid sequences but their functions are unknown. We analyzed them by yeast two-hybrid screens and found that they interact with the C-terminal region of the human chromatin-remodeling factor CHD-3 (chromo-helicase-DNA-binding domain protein-3). The interaction of CGI-55 and CHD-3 could be confirmed in vitro and in vivo by co-immunoprecipitations from Sf9 insect cells. Mapping showed that CGI-55 interacts with CHD-3 via two regions at its N- and C-terminals. The CGI-55 and Ki-1/57 mRNAs show highest expression in muscle, colon and kidney. A CGI55-GFP fusion protein was localized in the cytoplasm, nucleus and perinuclear regions of HeLa cells. These data suggest the possibility that CGI-55 and Ki-1/57 might be involved in nuclear functions like the remodeling of chromatin.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD30,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD44,
http://linkedlifedata.com/resource/pubmed/chemical/CHD3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/PAI-RBP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
533
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12505151-Adenosine Triphosphatases,
pubmed-meshheading:12505151-Amino Acid Sequence,
pubmed-meshheading:12505151-Animals,
pubmed-meshheading:12505151-Antigens, CD30,
pubmed-meshheading:12505151-Antigens, CD44,
pubmed-meshheading:12505151-Binding Sites,
pubmed-meshheading:12505151-Caenorhabditis elegans Proteins,
pubmed-meshheading:12505151-Chromatin,
pubmed-meshheading:12505151-DNA Helicases,
pubmed-meshheading:12505151-Gene Expression,
pubmed-meshheading:12505151-HeLa Cells,
pubmed-meshheading:12505151-Humans,
pubmed-meshheading:12505151-Molecular Sequence Data,
pubmed-meshheading:12505151-RNA, Messenger,
pubmed-meshheading:12505151-RNA-Binding Proteins,
pubmed-meshheading:12505151-Recombinant Proteins,
pubmed-meshheading:12505151-Sequence Homology, Amino Acid,
pubmed-meshheading:12505151-Tissue Distribution
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pubmed:year |
2003
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pubmed:articleTitle |
Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3.
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pubmed:affiliation |
Centro de Biologia Molecular Estrutural, Laboratório Nacional de Luz Si;ncrotron, Rua Giuseppe Máximo Scolfaro 10.000, C.P. 6192, 13084-971, Campinas, SP, Brazil.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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