cDNAs encoding the large subunit of human replication factor C.
- 1 December 1993
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 90 (23) , 11014-11018
- https://doi.org/10.1073/pnas.90.23.11014
Abstract
Replication factor C (RFC) is a multisubunit, DNA polymerase accessory protein required for the coordinated synthesis of both DNA strands during simian virus 40 DNA replication in vitro. Previous studies have shown that RFC is a DNA-dependent ATPase that binds in a structure-specific manner to the 39 end of a primer hybridized to a template DNA, an activity thought intrinsic to the 140-kDa component of this multisubunit complex. Here, the isolation and analysis of cDNAs encoding this subunit is described. Analysis of the full-length coding sequence revealed an open reading frame of 3.4 kb, encoding an 1148-amino acid protein with a predicted molecular mass of 130 kDa. A putative ATP-binding motif was observed that is similar to a motif in several of the smaller subunits of RFC and in functionally homologous replication factors of bacterial and viral origin. A "DEAD" box is also conserved among these proteins. The predicted protein shows significant identity with a DNA-binding protein of murine origin (B. Luckow, P. Lichter, and G. Schütz, personal communication). Regions of similarity were also seen between the amino acid sequences of the 140-kDa subunit of RFC, poly(ADP-ribose) polymerase, and bacterial DNA ligases--possibly representing a conserved structural feature of these proteins that bind similar DNA substrates.Keywords
This publication has 27 references indexed in Scilit:
- Protein-DNA cross-linking demonstrates stepwise ATP-dependent assembly of T4 DNA polymerase and its accessory proteins on the primer-templateCell, 1991
- Location of the active site for enzyme-adenylate formation in DNA ligases.Proceedings of the National Academy of Sciences, 1991
- Replication factors required for SV40 DNA replication in vitro. I. DNA structure-specific recognition of a primer-template junction by eukaryotic DNA polymerases and their accessory proteinsJournal of Biological Chemistry, 1991
- Studies on the activator 1 protein complex, an accessory factor for proliferating cell nuclear antigen-dependent DNA polymerase delta.Journal of Biological Chemistry, 1991
- Reconstitution of simian virus 40 DNA replication with purified proteins.Proceedings of the National Academy of Sciences, 1990
- Sequential initiation of lagging and leading strand synthesis by two different polymerase complexes at the SV40 DNA replication originNature, 1990
- Functions of replication factor C and proliferating-cell nuclear antigen: functional similarity of DNA polymerase accessory proteins from human cells and bacteriophage T4.Proceedings of the National Academy of Sciences, 1990
- Zinc-binding domain of poly(ADP-ribose)polymerase participates in the recognition of single strand breaks on DNAJournal of Molecular Biology, 1989
- STRUCTURAL AND ENZYMATIC STUDIES OF THE T4 DNA-REPLICATION SYSTEM .2. ATPASE PROPERTIES OF THE POLYMERASE ACCESSORY PROTEIN COMPLEX1989
- Purification of a cellular replication factor, RF-C, that is required for coordinated synthesis of leading and lagging strands during simian virus 40 DNA replication in vitro.Molecular and Cellular Biology, 1989