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).