The cloning and characterization of a cDNA encoding Xenopus laevis DNA ligase I.
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.
Lepetit
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Département de Biologie et Génétique du Développement, URA 256 CNRS, Université de Rennes I, France.
Thiebaud
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P
Aoufouchi
S
S
Prigent
C
C
Guesné
R
R
Thézé
N
N
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D000072481:DNA Ligase ATP; D011088:DNA Ligases / Q000235:genetics* / Q000378:metabolism; D018076:DNA, Complementary; D004625:Embryo, Nonmammalian / Q000201:enzymology; D004926:Escherichia coli; D008969:Molecular Sequence Data; D014982:Xenopus laevis
D018076:DNA, Complementary; D011088:DNA Ligases; D000072481:DNA Ligase ATP