Source:http://linkedlifedata.com/resource/pubmed/id/12045101
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2002-6-4
|
pubmed:abstractText |
Ubiquitous in eukaryotic cells, the La protein associates with the 3' termini of many newly synthesized small RNAs. RNAs bound by the La protein include all nascent transcripts made by RNA polymerase III as well as certain small RNAs synthesized by other RNA polymerases. Recent genetic and biochemical analyses have revealed that binding by the La protein protects the 3' ends of these RNAs from exonucleases. This La-mediated stabilization is required for the normal pathway of pre-tRNA maturation, facilitates assembly of small RNAs into functional RNA-protein complexes, and contributes to nuclear retention of certain small RNAs. Studies of mutant La proteins have given some insights into how the La protein specifically recognizes its RNA targets. However, many questions remain regarding the molecular mechanisms by which La protein binding influences multiple steps in small RNA biogenesis. This review focuses on the roles of the La protein in small RNA biogenesis and also discusses data that implicate the La protein in the translation of specific mRNAs.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase III,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/SS-B antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0066-4154
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
71
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
375-403
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:12045101-Adenosine Triphosphatases,
pubmed-meshheading:12045101-Amino Acid Sequence,
pubmed-meshheading:12045101-Animals,
pubmed-meshheading:12045101-Autoantigens,
pubmed-meshheading:12045101-Humans,
pubmed-meshheading:12045101-Molecular Sequence Data,
pubmed-meshheading:12045101-Phylogeny,
pubmed-meshheading:12045101-Protein Biosynthesis,
pubmed-meshheading:12045101-Protein Structure, Tertiary,
pubmed-meshheading:12045101-RNA,
pubmed-meshheading:12045101-RNA Polymerase III,
pubmed-meshheading:12045101-Ribonucleoproteins,
pubmed-meshheading:12045101-Sequence Alignment,
pubmed-meshheading:12045101-Transcription Factors
|
pubmed:year |
2002
|
pubmed:articleTitle |
The La protein.
|
pubmed:affiliation |
Departments of Cell Biology and Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, Connecticut 06536, USA. sandra.wolin@yale.edu
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
|