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Publication : Cloning, expression, and chromosomal localization of the 140-kilodalton subunit of replication factor C from mice and humans.

First Author  Luckow B Year  1994
Journal  Mol Cell Biol Volume  14
Issue  3 Pages  1626-34
PubMed ID  8114700 Mgi Jnum  J:16902
Mgi Id  MGI:64960 Doi  10.1128/mcb.14.3.1626
Citation  Luckow B, et al. (1994) Cloning, expression, and chromosomal localization of the 140-kilodalton subunit of replication factor C from mice and humans. Mol Cell Biol 14(3):1626-34
abstractText  We have isolated a full-length mouse cDNA encoding a lysine-rich protein of 1,131 amino acids with a calculated molecular mass of 126 kDa. The protein binds in a sequence-unspecific manner to DNA, is localized exclusively in the nucleus, and contains a putative ATP binding site and a stretch of 80 amino acids with homology to the carboxy terminus of prokaryotic DNA ligases. On the basis of the following facts, we conclude that the isolated cDNA encodes the 140-kDa subunit of mouse replication factor C (mRFC140). (i) The sequence around the ATP binding site shows significant homology to three small subunits of human replication factor C. (ii) Polyclonal antibodies raised against the protein encoded by this cDNA cross-react with the 140-kDa subunit of purified human replication factor C (hRFC140) and recognize in mouse cell extracts an authentic protein with an apparent molecular mass of 130 kDa. (iii) Sequence comparison with a human cDNA isolated by using tryptic peptide sequence information from purified hRFC140 revealed 83% identity of the encoded proteins. The mRFC140 gene is ubiquitously expressed, and two mRNAs approximately 5.0 and 4.5 kb long have been detected. The gene was mapped by in situ hybridization to mouse chromosome 5, and its human homolog was mapped to chromosome 4 (p13-p14).
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