Document Detail

A 54-kDa fragment of the Poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting Poly(A)-specific 3' exonuclease.
MedLine Citation:
PMID:  10801819     Owner:  NLM     Status:  MEDLINE    
We have previously identified a HeLa cell 3' exonuclease specific for degrading poly(A) tails of mRNAs. Here we report on the purification and identification of a calf thymus 54-kDa polypeptide associated with a similar 3' exonuclease activity. The 54-kDa polypeptide was shown to be a fragment of the poly(A)-specific ribonuclease 74-kDa polypeptide. The native molecular mass of the nuclease activity was estimated to be 180-220 kDa. Protein/protein cross-linking revealed an oligomeric structure, most likely consisting of three subunits. The purified nuclease activity released 5'-AMP as the reaction product and degraded poly(A) in a highly processive fashion. The activity required monovalent cations and was dependent on divalent metal ions. The RNA substrate requirement was investigated, and it was found that the nuclease was highly poly(A)-specific and that only 3' end-located poly(A) was degraded by the activity. RNA substrates capped with m(7)G(5')ppp(5')G were more efficiently degraded than noncapped RNA substrates. Addition of free m(7)G(5')ppp(5')G cap analogue inhibited poly(A) degradation in vitro, suggesting a functional link between the RNA 5' end cap structure and poly(A) degradation at the 3' end of the RNA.
J Martinez; Y G Ren; A C Thuresson; U Hellman; J Astrom; A Virtanen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  275     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2000 Aug 
Date Detail:
Created Date:  2000-09-07     Completed Date:  2000-09-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  24222-30     Citation Subset:  IM    
Department of Cell and Molecular Biology, Uppsala University, Box 596, SE-751 24 Uppsala, Sweden.
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MeSH Terms
Adenosine Monophosphate / metabolism
Chromatography, Affinity / methods
Exoribonucleases / isolation & purification,  metabolism*
Peptide Fragments / metabolism
Protein Binding
Protein Structure, Quaternary
RNA Caps / metabolism*
RNA Processing, Post-Transcriptional
Substrate Specificity
Thymus Gland / enzymology*
Reg. No./Substance:
0/Peptide Fragments; 0/RNA Caps; 61-19-8/Adenosine Monophosphate; EC 3.1.-/Exoribonucleases; EC ribonuclease

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