Document Detail


Proteomic and functional analysis of the noncanonical poly(A) polymerase Cid14.
MedLine Citation:
PMID:  20403971     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The fission yeast Cid14 protein belongs to a family of noncanonical poly(A) polymerases which have been implicated in a broad range of biological functions. Here we describe an extensive Cid14 protein-protein interaction network and its biochemical dissection. Cid14 most stably interacts with the zinc-knuckle protein Air1 to form the Cid14-Air1 complex (CAC). Providing a link to ribosomal RNA processing, Cid14 sediments with 60S ribosomal subunits and copurifies with 60S assembly factors. In contrast, no physical link to chromatin has been identified, although gene expression profiling revealed that efficient silencing of a few heterochromatic genes depends on Cid14 and/or Air1.
Authors:
Claudia Keller; Katrina Woolcock; Daniel Hess; Marc Bühler
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-04-19
Journal Detail:
Title:  RNA (New York, N.Y.)     Volume:  16     ISSN:  1469-9001     ISO Abbreviation:  RNA     Publication Date:  2010 Jun 
Date Detail:
Created Date:  2010-05-24     Completed Date:  2010-07-07     Revised Date:  2011-03-03    
Medline Journal Info:
Nlm Unique ID:  9509184     Medline TA:  RNA     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1124-9     Citation Subset:  IM    
Affiliation:
Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058 Basel, Switzerland.
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MeSH Terms
Descriptor/Qualifier:
Chromatin / genetics,  metabolism
Cycloheximide / metabolism
Gene Expression Regulation, Fungal
Kinetics
Molecular Weight
Polynucleotide Adenylyltransferase / chemistry*,  metabolism
Polyribosomes / metabolism
Puromycin / metabolism
RNA, Fungal / genetics,  metabolism
RNA, Ribosomal / genetics,  metabolism
Schizosaccharomyces / enzymology
Schizosaccharomyces pombe Proteins / chemistry*,  metabolism
Chemical
Reg. No./Substance:
0/Chromatin; 0/RNA, Fungal; 0/RNA, Ribosomal; 0/Schizosaccharomyces pombe Proteins; 53-79-2/Puromycin; 66-81-9/Cycloheximide; EC 2.7.7.19/Cid14 protein, S pombe; EC 2.7.7.19/Polynucleotide Adenylyltransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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