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. 1996 Jun 26;172(2):273-7.
doi: 10.1016/0378-1119(96)00175-8.

The cloning and characterization of a cDNA encoding Xenopus laevis DNA ligase I

D Lepetit  1 , P Thiebaud, S Aoufouchi, C Prigent, R Guesné, N Thézé
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The cloning and characterization of a cDNA encoding Xenopus laevis DNA ligase I

D Lepetit et al. Gene. .

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.

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