The human DNA-binding protein, PO-GA, is homologous to the large subunit of mouse replication factor C: regulation by alternate 3′ processing of mRNA

Gene ◽  
1994 ◽  
Vol 145 (2) ◽  
pp. 261-265 ◽  
Author(s):  
Lu Yang ◽  
Anna Tate Riegel
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Large Subunit ◽  
Dna Binding Protein ◽  
Replication Factor C ◽  
Replication Factor ◽  
Human Dna ◽  
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 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 Sequence Elements in both the Intergenic Space and the 3′ Untranslated Region of the Crithidia fasciculata KAP3 Gene Are Required for Cell Cycle Regulation of KAP3 mRNA

2003 ◽  
Vol 2 (4) ◽  
pp. 671-677 ◽  
Author(s):  
Nuraly K. Avliyakulov ◽  
Jane C. Hines ◽  
Dan S. Ray
Keyword(s):  
Cell Cycle ◽  
Dna Binding ◽  
Binding Protein ◽  
Large Subunit ◽  
Dna Binding Protein ◽  
Mrna Levels ◽  
Crithidia Fasciculata ◽  
Consensus Sequences ◽  
Transcript Processing ◽  
Cycle Dependent

ABSTRACT mRNA levels of several Crithidia fasciculata genes involved in DNA metabolism have previously been found to cycle as cells progress through the cell cycle. Octamer consensus sequences in the 5′ untranslated regions (5′ UTRs) of these transcripts were shown to be required for cycling of these mRNAs. The KAP3 gene encodes a kinetoplast histone H1-like DNA binding protein, and its mRNA levels cycle in parallel with those of the kinetoplast DNA topoisomerase (TOP2), dihydrofolate reductase-thymidylate synthase (DHFR-TS), and the large subunit of the nuclear single-stranded DNA binding protein (RPA1). KAP3 mRNA contains two octamer consensus sequences in its 3′ UTR but none in its 5′ UTR. Mutation of these octamer sequences was not sufficient to prevent cycling of a sequence-tagged KAP3 mRNA expressed from a plasmid. Mutation of an octamer sequence contained on the precursor transcript but not on the mRNA, in addition to mutation of the two octamer sequences in the 3′ UTR, was necessary to abolish cycling of the mRNA. The requirement for a sequence not present on the mature mRNA indicates that regulation of the mRNA levels by the octamer sequences occurs at or prior to splicing of the transcript. Incompletely processed RNAs containing octamer sequences were also found to accumulate during the cell cycle when the mRNA levels were lowest. These RNA species hybridize to both the KAP3 coding sequence and that of the downstream drug resistance gene, indicating a lack of processing within the intergenic region separating these genes. We propose a cell cycle-dependent interference in transcript processing mediated by octamer consensus sequences as a mechanism contributing to the cycling of such transcripts.

Unravelling the Function of Human DNA-Binding Protein Par14 in the Cellular Nucleus

2008 ◽  
Vol 2008 (Spring) ◽  
Author(s):  
Akuma Divine Saningong ◽  
Peter Bayer ◽  
Jonathan Wolf Mueller
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Human Dna

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.

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