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Comparative Study
. 1993 Dec 15;90(24):11543-7.
doi: 10.1073/pnas.90.24.11543.

Cloning of the large subunit of activator 1 (replication factor C) reveals homology with bacterial DNA ligases

P D Burbelo  1 , A Utani, Z Q Pan, Y Yamada
Affiliations
Comparative Study

Cloning of the large subunit of activator 1 (replication factor C) reveals homology with bacterial DNA ligases

P D Burbelo et al. Proc Natl Acad Sci U S A. .

Abstract

We have cloned a gene encoding a DNA-binding protein by Southwestern screening of a murine cDNA library with a double-stranded oligonucleotide containing the sequence from the bidirectional promoter of the alpha 1 and alpha 2 collagen IV genes. The middle portion of this 1131-amino acid protein has a region homologous to bacterial DNA ligases, and the more carboxyl portion contains several domains homologous to p40, p38, p37, and p36.5 subunits of activator 1 (A1, also called replication factor C), a human replication protein complex. Western blotting revealed that antiserum generated against part of the recombinant protein reacted specifically with the 145-kDa component of the purified human A1 complex, indicating that it is the murine counterpart of the A1 p145. Characterization of the DNA-binding activity of the recombinant fusion protein by gel mobility-shift assay revealed that it had a preference for a run of pyrimidines on one strand. Deletion analysis using recombinant proteins revealed that the DNA ligase-like domain was required for DNA-binding activity. The finding that the region required for the binding of murine A1 p145 to DNA has similarity to a domain found in DNA ligases suggests that this region may be utilized by both proteins in recognizing DNA.

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