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

David Lepetit; Pierre Thiebaud; Saïd Aoufouchi; Claude Prigent; Rozène Guesné; Nadine Thézé

doi:10.1016/0378-1119(96)00175-8

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

David Lepetit, Pierre Thiebaud, Saïd Aoufouchi, Claude Prigent, Rozène Guesné, Nadine Thézé

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4 Citations (Scopus)

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.

Original language	English
Pages (from-to)	273-277
Number of pages	5
Journal	Gene
Volume	172
Issue number	2
DOIs	https://doi.org/10.1016/0378-1119(96)00175-8
Publication status	Published - 26 Jun 1996
Externally published	Yes

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title = "The cloning and characterization of a cDNA encoding Xenopus laevis DNA ligase I",

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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AU - Lepetit, David

AU - Thiebaud, Pierre

AU - Aoufouchi, Saïd

AU - Prigent, Claude

AU - Guesné, Rozène

AU - Thézé, Nadine

PY - 1996/6/26

Y1 - 1996/6/26

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

Abstract

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