rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1998-4-9
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pubmed:databankReference |
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pubmed:abstractText |
High-affinity binding of a set of proteins with specificity for the 5' untranslated region (UTR) of the Chlamydomonas reinhardtii chloroplast psbA mRNA correlates with light-regulated translational activation of this message. We have isolated a cDNA encoding the main psbA RNA binding protein, RB47, and identified this protein as a member of the poly(A) binding protein family. Poly(A) binding proteins are a family of eukaryotic, cytoplasmic proteins thought to bind poly(A) tails of mRNAs and play a role in translational regulation. In vitro translation of RNA transcribed from the RB47 cDNA produces a precursor protein that is efficiently transported into the chloroplast and processed to the mature 47-kDa protein. RB47 expressed and purified from Escherichia coli binds to the psbA 5' UTR with similar specificity and affinity as RB47 isolated from C. reinhardtii chloroplasts. The identification of a normally cytoplasmic translation factor in the chloroplast suggests that the prokaryotic-like chloroplast translation machinery utilizes a eukaryotic-like initiation factor to regulate the translation of a key chloroplast mRNA. These data also suggest that poly(A) binding proteins may play a wider role in translation regulation than previously appreciated.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9482869-1282351,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9482869-1292669,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/9482869-9395399
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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 |
Mar
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
95
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2238-43
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9482869-Animals,
pubmed-meshheading:9482869-Chloroplasts,
pubmed-meshheading:9482869-Protein Biosynthesis,
pubmed-meshheading:9482869-RNA, Messenger,
pubmed-meshheading:9482869-Amino Acid Sequence,
pubmed-meshheading:9482869-Binding Sites,
pubmed-meshheading:9482869-Molecular Sequence Data,
pubmed-meshheading:9482869-Transcription, Genetic,
pubmed-meshheading:9482869-Cloning, Molecular,
pubmed-meshheading:9482869-Sequence Alignment,
pubmed-meshheading:9482869-Sequence Homology, Amino Acid,
pubmed-meshheading:9482869-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:9482869-Photosystem II Protein Complex,
pubmed-meshheading:9482869-Chlamydomonas reinhardtii,
pubmed-meshheading:9482869-Recombinant Proteins,
pubmed-meshheading:9482869-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:9482869-RNA-Binding Proteins,
pubmed-meshheading:9482869-Poly(A)-Binding Proteins
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