Cloning of the murine cDNA encoding VDJP, a protein homologous to the large subunit of replication factor C and bacterial DNA ligases

A putative full-length 1.7-kb cDNA, encoding a murine protein that specifically binds to the nonamer portion of the V(D)J recombinational signal sequence ( RSS) element, has been cloned. By its sequence analysis, this cDNA is identical to a portion of the 4.5-kb murine replication factor C large-sub...

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Bibliographic Details
Published in:Gene 1995-08, Vol.161 (2), p.217-222
Main Authors: Halligan, Brian D., Teng, Ming, Guilliams, Thomas G., Nauert, J.Brian, Halligan, Nadine L.N.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Binding Sites
DNA Ligases - genetics
DNA Nucleotidyltransferases - biosynthesis
DNA Nucleotidyltransferases - genetics
DNA recombination
DNA Replication
DNA, Complementary - genetics
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
Escherichia coli - genetics
Homeodomain Proteins
Mice
Minor Histocompatibility Antigens
Molecular Sequence Data
Mutation
Protein Conformation
protein homology
Proto-Oncogene Proteins c-bcl-2
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - genetics
Replication Protein C
Repressor Proteins
Saccharomyces cerevisiae Proteins
Sequence Homology, Nucleic Acid
VDJ Recombinases
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Summary:A putative full-length 1.7-kb cDNA, encoding a murine protein that specifically binds to the nonamer portion of the V(D)J recombinational signal sequence ( RSS) element, has been cloned. By its sequence analysis, this cDNA is identical to a portion of the 4.5-kb murine replication factor C large-subunit-encoding cDNA. By Northern blot analysis, the 1.7-kb mRNA species is observed in murine immature B cells but not in non-lymphoid cells and tissues, while the 4.5-kb replication factor C-encoding cDNA is expressed in all cell types. The deduced VDJP amino-acid sequence includes a region of homology with bacterial DNA ligases at the C terminus of each of the proteins. VDJP has been synthesized as a fusion protein in bacteria, and the purified protein has been previously shown to mediate the joining of DNA fragments in a V(D)J RSS-dependent fashion (Guilliams et al., Biochem. Biophys. Res. Commun. 202 (1994) 1134-1141).
ISSN:0378-1119
1879-0038
DOI:10.1016/0378-1119(95)00299-L