2019-01-16T11:06:48Z
2019-01-16T11:06:48Z
1989
2019-01-16T11:06:48Z
The amino-terminal fragment of the RecA protein was cloned in pUA27 plasmid and introduced in different repair mutants of Escherichia coli. The UV-mediated induction of several SOS functions was then studied. Results show that the truncated RecA protein plays an important role in the UV-damaged DNA when the level of the chromosomal RecA protein is low. Furthermore, RecA protein inhibited the protease activity of the wild type RecA protein causing a decrease in the SOS system induction. All these data suggest that hybrid tetramers between both truncated and wild type RecA proteins may be formed, and as a consequence the ATPase capacity and active conformation of the wild type RecA protein are blocked.
Article
Published version
Catalan
Duplicació de l'ADN; Escheríchia coli; Reparació de l'ADN; DNA replication; Escherichia coli; DNA repair
Societat Catalana de Biologia
Reproducció del document publicat a: https://www.raco.cat/index.php/TreballsSCBiologia/article/view/238113/
Treballs de la Societat Catalana de Biologia, 1989, vol. 40, p. 33-46
cc-by-nc-nd (c) Barbé García, Jordi et al., 1989
http://creativecommons.org/licenses/by-nc-nd/3.0/es