Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/95989
Type: Artigo de periódico
Title: Characterisation Of A Gain-of-function Mutant Of Poly(adp-ribose) Polymerase
Author: Miranda E.A.
Dantzer F.
O'Farrell M.
De Murcia G.
De Murcia J.M.
Abstract: In order to examine the stucture-function relationship of the poly (ADP-ribose) polymerase (PARP) catalytic domain, potential active-site residues in the catalytic domain have previously been described. Here, we have used mutagenesis with hydroxylamine to generate a random library of PARP mutants. The identification, overproduction in insect cells, purification and characterization of a gain-of-function mutant (L713F) is described. We show that the k(cat) of this mutant is increased over nine times compared to the wild-type enzyme; the K(m) for NAD+ is unchanged. The size and the branching structure of the ADP-ribose polymers are similar in both the wild-type and the mutant enzyme. This mutation may have an allosteric effect on the catalytic site and could be useful in analyzing the consequences of poly ADP-ribose overproduction in vivo on cell survival following DNA damage.
Editor: 
Rights: fechado
Identifier DOI: 10.1006/bbrc.1995.1972
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0029119615&partnerID=40&md5=da8c6896f9b066eb43b169f4e1872850
Date Issue: 1995
Appears in Collections:Unicamp - Artigos e Outros Documentos

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