rdf:type |
|
lifeskim:mentions |
umls-concept:C0003593,
umls-concept:C0009017,
umls-concept:C0035696,
umls-concept:C0085177,
umls-concept:C0205314,
umls-concept:C0679622,
umls-concept:C0868955,
umls-concept:C1314754,
umls-concept:C1314939,
umls-concept:C1412472,
umls-concept:C1521761
|
pubmed:issue |
5
|
pubmed:dateCreated |
2000-3-16
|
pubmed:abstractText |
The C-to-U editing of apolipoprotein B (apo-B) mRNA is catalyzed by a multiprotein complex that recognizes an 11-nucleotide mooring sequence downstream of the editing site. The catalytic subunit of the editing enzyme, apobec-1, has cytidine deaminase activity but requires additional unidentified proteins to edit apo-B mRNA. We purified a 65-kDa protein that functionally complements apobec-1 and obtained peptide sequence information which was used in molecular cloning experiments. The apobec-1 complementation factor (ACF) cDNA encodes a novel 64.3-kDa protein that contains three nonidentical RNA recognition motifs. ACF and apobec-1 comprise the minimal protein requirements for apo-B mRNA editing in vitro. By UV cross-linking and immunoprecipitation, we show that ACF binds to apo-B mRNA in vitro and in vivo. Cross-linking of ACF is not competed by RNAs with mutations in the mooring sequence. Coimmunoprecipitation experiments identified an ACF-apobec-1 complex in transfected cells. Immunodepletion of ACF from rat liver extracts abolished editing activity. The immunoprecipitated complexes contained a functional holoenzyme. Our results support a model of the editing enzyme in which ACF binds to the mooring sequence in apo-B mRNA and docks apobec-1 to deaminate its target cytidine. The fact that ACF is widely expressed in human tissues that lack apobec-1 and apo-B mRNA suggests that ACF may be involved in other RNA editing or RNA processing events.
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pubmed:grant |
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-1371931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-1400437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-1464582,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-1649450,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-1885564,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-1996349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-2216773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-2254300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-2758465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-3621347,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-3659919,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-7510636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-7736571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-7782342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-7862132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-7926751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-8036511,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-8999813,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-9175473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-9326486,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/10669759-9792439
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Mar
|
pubmed:issn |
0270-7306
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
1846-54
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10669759-Amino Acid Sequence,
pubmed-meshheading:10669759-Animals,
pubmed-meshheading:10669759-Apolipoproteins B,
pubmed-meshheading:10669759-Cloning, Molecular,
pubmed-meshheading:10669759-Cytidine Deaminase,
pubmed-meshheading:10669759-DNA, Complementary,
pubmed-meshheading:10669759-Humans,
pubmed-meshheading:10669759-Molecular Sequence Data,
pubmed-meshheading:10669759-RNA, Messenger,
pubmed-meshheading:10669759-RNA Editing,
pubmed-meshheading:10669759-RNA-Binding Proteins,
pubmed-meshheading:10669759-Rats
|
pubmed:year |
2000
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pubmed:articleTitle |
Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA.
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pubmed:affiliation |
Department of Cell Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA.
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pubmed:publicationType |
Journal Article
|