Document Detail


Translational regulation of ribonucleotide reductase by eukaryotic initiation factor 4E links protein synthesis to the control of DNA replication.
MedLine Citation:
PMID:  10585489     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Ribonucleotide reductase synthesizes dNDPs, a specific and limiting step in DNA synthesis, and can participate in neoplastic transformation when overexpressed. The small subunit (ribonucleotide reductase 2 (RNR2)) was cloned as a major product in a subtraction library from eukaryotic initiation factor 4E (eIF4E)-transformed cells (Chinese hamster ovary-4E (CHO-4E)). CHO-4E cells have 20-40-fold elevated RNR2 protein, reflecting an increased distribution of RNR2 mRNA to the heavy polysomes. CHO-4E cells display an altered cell cycle with shortened S phase, similar to cells selected for RNR2 overexpression with hydroxyurea. The function of ribonucleotide reductase as a checkpoint component of S progression was studied in yeast in which elevated eIF4E rescued S-arrested rnr2-68(ts) cells, by increasing recruitment of its mRNA to polysomes. Crosses between rnr2-68(ts) and mutant eIF4E (cdc33-1(ts)) engendered conditional synthetic lethality, with extreme sensitivity to hydroxyurea and the microtubule depolymerizing agent, benomyl. The double mutant (cdc33-1 rnr2-68) also identified a unique terminal phenotype, arrested with small bud and a randomly distributed single nucleus, which is distinct from those of both parental single mutants. This phenotype defines eIF4E and RNR2 as determinants in an important cell cycle checkpoint, in early/mid-S phase. These results also provide a link between protein and DNA synthesis and provide an explanation for cell cycle alterations induced by elevated eIF4E.
Authors:
M R Abid; Y Li; C Anthony; A De Benedetti
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  274     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1999 Dec 
Date Detail:
Created Date:  2000-01-13     Completed Date:  2000-01-13     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  35991-8     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Louisiana State University Medical Center, Shreveport, Louisiana 71130-3932, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Benomyl / pharmacology
CHO Cells
Cell Cycle / physiology
Cloning, Molecular
Cricetinae
DNA Replication*
Eukaryotic Initiation Factor-4E
Fibroblast Growth Factors / genetics
Gene Expression Regulation* / drug effects
Hydroxyurea / pharmacology
Microtubules / drug effects,  ultrastructure
Ornithine Decarboxylase / genetics
Peptide Initiation Factors / genetics,  metabolism*
Polyribosomes / metabolism
Protein Biosynthesis*
RNA, Messenger / genetics
Recombinant Proteins / metabolism
Ribonucleotide Reductases / biosynthesis,  genetics*
S Phase
Saccharomyces cerevisiae / genetics
Transcription, Genetic*
Transfection
Grant Support
ID/Acronym/Agency:
CA69148/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Eukaryotic Initiation Factor-4E; 0/Peptide Initiation Factors; 0/RNA, Messenger; 0/Recombinant Proteins; 127-07-1/Hydroxyurea; 17804-35-2/Benomyl; 62031-54-3/Fibroblast Growth Factors; EC 1.17.4.-/Ribonucleotide Reductases; EC 4.1.1.17/Ornithine Decarboxylase

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


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