Abstract : A cDNA clone coding for DNA ligase I (LigI) was isolated from a Xenopus laevis oocyte cDNA library. The 3766-bp sequence showed a putative ORF capable of encoding a 1070-amino-acid protein whose overall identity with two mammalian sequences is 63%. This identity, however, rises to 72.5% in the C-terminal portion of the protein that contains the active site. Expression of the cDNA in a prokaryotic system produces a protein that is immunologically identical to LigI and can be adenylated. The 180-kDa size of the recombinant protein is similar to the LigI detected in oocyte. Northern blot analysis of ovary and embryo RNAs revealed the expression of two (4.1 and 6 kb) LigI transcripts.
http://www.hal.inserm.fr/inserm-00966032
Contributeur : Claude Prigent
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Soumis le : mercredi 26 mars 2014 - 08:41:02
Dernière modification le : mercredi 16 mai 2018 - 11:24:08
David Lepetit, Pierre Thiebaud, Saïd Aoufouchi, Claude Prigent, Rozène Guesné, et al.. The cloning and characterization of a cDNA encoding Xenopus laevis DNA ligase I.. Gene, Elsevier, 1996, 172 (2), pp.273-7. 〈inserm-00966032〉
