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1996-02-26
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Document 0230
DOCN M9620230
TI Catalytic editing properties of DNA polymerases.
DT 9602
AU Canard B; Cardona B; Sarfati RS; Faculte de Medecine, Unite de Recherche
Associee-Centre; National de la Recherche Scientifique 1462, Nice,
France.
SO Proc Natl Acad Sci U S A. 1995 Nov 21;92(24):10859-63. Unique Identifier
: AIDSLINE MED/96074606
AB Enzymatic incorporation of 2',3'-dideoxynucleotides into DNA results in
chain termination. We report that 3'-esterified 2'-deoxynucleoside
5'-triphosphates (dNTPs) are false chain-terminator substrates since DNA
polymerases, including human immunodeficiency virus reverse
transcriptase, can incorporate them into DNA and, subsequently, use this
new 3' end to insert the next correctly paired dNTP. Likewise, a DNA
substrate with a primer chemically esterified at the 3' position can be
extended efficiently upon incubation with dNTPs and T7 DNA polymerase
lacking 3'-to-5' exonuclease activity. This enzyme is also able to use
dTTP-bearing reporter groups in the 3' position conjugated through amide
or thiourea bonds and cleave them to restore a DNA chain terminated by
an amino group at the 3' end. Hence, a number of DNA polymerases exhibit
wide catalytic versatility at the 3' end of the nascent DNA strand. As
part of the polymerization mechanism, these capabilities extend the
number of enzymatic activities associated with these enzymes and also
the study of interactions between DNA polymerases and nucleotide
analogues.
DE Base Sequence DNA/*BIOSYNTHESIS DNA Polymerases/*METABOLISM DNA
Primers/CHEMISTRY Hydrolysis Molecular Sequence Data RNA-Directed DNA
Polymerase/*METABOLISM Substrate Specificity Support, Non-U.S. Gov't
JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).