scholarly journals Chromosomal localization of the large subunit of mouse replication factor C in the mouse and human

1995 ◽  
Vol 6 (1) ◽  
pp. 58-59 ◽  
Author(s):  
A. C. Lossie ◽  
B. R. Haugen ◽  
W. M. Wood ◽  
S. A. Camper ◽  
D. F. Gordon
Keyword(s):  
Chromosomal Localization ◽  
Large Subunit ◽  
Replication Factor C ◽  
Replication Factor ◽  
Factor C

scholarly journals The Large Subunit of Replication Factor C (Rfclp/Cdc44p) Is Required for DNA Replication and DNA Repair in Saccharomyces cerevisiae

Genetics ◽  
1996 ◽  
Vol 142 (1) ◽  
pp. 65-78 ◽  
Author(s):  
Michael A McAlear ◽  
K Michelle Tuffo ◽  
Connie Holm
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Repair ◽  
Dna Replication ◽  
Uv Radiation ◽  
Large Subunit ◽  
Restrictive Temperature ◽  
Replication Factor C ◽  
Replication Factor ◽  
Factor C

We used genetic and biochemical techniques to characterize the phenotypes associated with mutations affecting the large subunit of replication factor C (Cdc44p or Rfc1p) in Saccharomyces cerevisiae. We demonstrate that Cdc44p is required for both DNA replication and DNA repair in vivo. Cold-sensitive cdc44 mutants experience a delay in traversing S phase at the restrictive temperature following alpha factor arrest; although mutant cells eventually accumulate with a G2/M DNA content, they undergo a cell cycle arrest and initiate neither mitosis nor a new round of DNA synthesis. cdc44 mutants also exhibit an elevated level of spontaneous mutation, and they are sensitive both to the DNA damaging agent methylmethane sulfonate and to exposure to UV radiation. After exposure to UV radiation, cdc44 mutants at the restrictive temperature contain higher levels of single-stranded DNA breaks than do wild-type cells. This observation is consistent with the hypothesis that Cdc44p is involved in repairing gaps in the DNA after the excision of damaged bases. Thus, Cdc44p plays an important role in both DNA replication and DNA repair in vivo.

scholarly journals CDC44: a putative nucleotide-binding protein required for cell cycle progression that has homology to subunits of replication factor C.

1994 ◽  
Vol 14 (1) ◽  
pp. 255-267 ◽  
Author(s):  
E A Howell ◽  
M A McAlear ◽  
D Rose ◽  
C Holm
Keyword(s):  
Cell Cycle ◽  
Dna Damage ◽  
Cell Cycle Arrest ◽  
Large Subunit ◽  
Mitotic Cell ◽  
Predicted Amino Acid Sequence ◽  
Replication Factor C ◽  
Replication Factor ◽  
Cycle Arrest ◽  
Factor C

To investigate the means by which a cell regulates the progression of the mitotic cell cycle, we characterized cdc44, a mutation that causes Saccharomyces cerevisiae cells to arrest before mitosis. CDC44 encodes a 96-kDa basic protein with significant homology to a human protein that binds DNA (PO-GA) and to three subunits of human replication factor C (also called activator 1). The hypothesis that Cdc44p is involved in DNA metabolism is supported by the observations that (i) levels of mitotic recombination suggest elevated rates of DNA damage in cdc44 mutants and (ii) the cell cycle arrest observed in cdc44 mutants is alleviated by the DNA damage checkpoint mutations rad9, mec1, and mec2. The predicted amino acid sequence of Cdc44p contains GTPase consensus sites, and mutations in these regions cause a conditional cell cycle arrest. Taken together, these observations suggest that the essential CDC44 gene may encode the large subunit of yeast replication factor C.

scholarly journals cDNAs encoding the large subunit of human replication factor C

1993 ◽  
Vol 90 (23) ◽  
pp. 11014-11018 ◽  
Author(s):  
F Bunz ◽  
R Kobayashi ◽  
B Stillman
Keyword(s):  
Amino Acid ◽  
Large Subunit ◽  
Simian Virus 40 ◽  
Amino Acid Sequences ◽  
Binding Motif ◽  
Replication Factor C ◽  
Viral Origin ◽  
Replication Factor ◽  
Factor C

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 3' 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.

scholarly journals Regulation of RelA (p65) Function by the Large Subunit of Replication Factor C

2003 ◽  
Vol 23 (2) ◽  
pp. 721-732 ◽  
Author(s):  
Lisa A. Anderson ◽  
Neil D. Perkins
Keyword(s):  
Tumor Suppressor ◽  
Large Subunit ◽  
Dominant Negative ◽  
Nuclear Antigen ◽  
Replication Factor C ◽  
Clamp Loader ◽  
Replication Factor ◽  
Factor C

ABSTRACT The RelA (p65) subunit of NF-κB is an important regulator of inflammation, proliferation, and apoptosis. We have discovered that the large subunit, p140, of replication factor C (RFC) can function as a regulator of RelA. RFC is a clamp loader, facilitating the addition and removal of proliferating-cell nuclear antigen from DNA during replication and repair but can also interact directly with the retinoblastoma tumor suppressor protein and the transcription factor C/EBPα. We find that RFC (p140) interacts with RelA both in vitro and in vivo and stimulates RelA transactivation. In contrast, coexpression of fragments of RFC (p140) that mediate the interaction with RelA results in transcriptional inhibition. The significance of this regulation was confirmed by using short interfering RNA oligonucleotides targeted to RFC (p140). Down regulation of endogenous RFC (p140) inhibits expression from a chromosomally integrated reporter plasmid induced by endogenous, TNF-α-activated NF-κB. Dominant negative fragments of RFC (p140) also cooperate with overexpressed RelA to induce cell death. Interestingly, RFC (p140) also interacts with the tumor suppressor p53. Taken together, these observations suggest that, in addition to its previously described function in DNA replication and repair, RFC (p140) has an important role as a regulator of transcription and NF-κB activity.

CDC44: a putative nucleotide-binding protein required for cell cycle progression that has homology to subunits of replication factor C

1994 ◽  
Vol 14 (1) ◽  
pp. 255-267
Author(s):  
E A Howell ◽  
M A McAlear ◽  
D Rose ◽  
C Holm
Keyword(s):  
Cell Cycle ◽  
Dna Damage ◽  
Cell Cycle Arrest ◽  
Large Subunit ◽  
Mitotic Cell ◽  
Predicted Amino Acid Sequence ◽  
Replication Factor C ◽  
Replication Factor ◽  
Cycle Arrest ◽  
Factor C

To investigate the means by which a cell regulates the progression of the mitotic cell cycle, we characterized cdc44, a mutation that causes Saccharomyces cerevisiae cells to arrest before mitosis. CDC44 encodes a 96-kDa basic protein with significant homology to a human protein that binds DNA (PO-GA) and to three subunits of human replication factor C (also called activator 1). The hypothesis that Cdc44p is involved in DNA metabolism is supported by the observations that (i) levels of mitotic recombination suggest elevated rates of DNA damage in cdc44 mutants and (ii) the cell cycle arrest observed in cdc44 mutants is alleviated by the DNA damage checkpoint mutations rad9, mec1, and mec2. The predicted amino acid sequence of Cdc44p contains GTPase consensus sites, and mutations in these regions cause a conditional cell cycle arrest. Taken together, these observations suggest that the essential CDC44 gene may encode the large subunit of yeast replication factor C.

scholarly journals Cell Cycle-dependent Phosphorylation of the Large Subunit of Replication Factor C (RF-C) Leads to Its Dissociation from the RF-C Complex

2003 ◽  
Vol 278 (48) ◽  
pp. 48467-48473 ◽  
Author(s):  
Anil Munshi ◽  
Dominique Cannella ◽  
Howard Brickner ◽  
Isabelle Salles-Passador ◽  
Vladimir Podust ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Large Subunit ◽  
Replication Factor C ◽  
Replication Factor ◽  
C Complex ◽  
Cycle Dependent ◽  
Factor C
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