Document Detail


Inhibition by aphidicolin and dideoxythymidine triphosphate of a multienzyme complex of DNA synthesis from human cells.
MedLine Citation:
PMID:  6409668     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A multienzyme complex consisting of DNA polymerase and several DNA precursor-synthesizing enzymes was solubilized by gentle lysis of cultured human cells. This complex channelled the distal precursor [3H]dTMP into DNA. The patterns of inhibition of the complex by aphidicolin and dideoxythymidine triphosphate (ddTTP) suggested that the complex contained the replicative DNA polymerase, polymerase alpha. Inhibition by ddTTP was competitive with dTTP. This was exploited to estimate the effective concentration of [3H]dTTP at the site of DNA synthesis during channelling of [3H]dTMP into DNA. The estimated concentration (about 50 microM) was so high as to suggest that the solubilized complex was able to functionally compartmentalize DNA precursors.
Authors:
R G Wickremasinghe; A V Hoffbrand
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  159     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1983 Aug 
Date Detail:
Created Date:  1983-09-20     Completed Date:  1983-09-20     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  175-9     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Aphidicolin
DNA Replication / drug effects*
DNA-Directed DNA Polymerase / metabolism
Dideoxynucleotides
Diterpenes / pharmacology*
Humans
Multienzyme Complexes / metabolism
Thymine Nucleotides / metabolism,  pharmacology*
Chemical
Reg. No./Substance:
0/Dideoxynucleotides; 0/Diterpenes; 0/Multienzyme Complexes; 0/Thymine Nucleotides; 365-08-2/thymidine 5'-triphosphate; 38966-21-1/Aphidicolin; 611-60-9/2',3'-dideoxythymidine triphosphate; EC 2.7.7.7/DNA-Directed DNA Polymerase

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


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