Short Communication Molecular Cloning of a Chick Cochlea cDNA Encoding a Subunit of DNA Replication Factor C/Activator 1

1994 ◽  
Vol 13 (8) ◽  
pp. 857-863 ◽  
Author(s):  
J. CARL OBERHOLTZER ◽  
ERIK L. COHEN ◽  
JAMES G. DAVIS
Keyword(s):  
Dna Replication ◽  
Molecular Cloning ◽  
Short Communication ◽  
Replication Factor C ◽  
Replication Factor ◽  
A Subunit ◽  
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 Mechanical Link between Cohesion Establishment and DNA Replication: Ctf7p/Eco1p, a Cohesion Establishment Factor, Associates with Three Different Replication Factor C Complexes

2003 ◽  
Vol 23 (8) ◽  
pp. 2999-3007 ◽  
Author(s):  
Margaret A. Kenna ◽  
Robert V. Skibbens
Keyword(s):  
Dna Replication ◽  
Replication Factor C ◽  
Biologically Relevant ◽  
Replication Factor ◽  
Chromatid Cohesion ◽  
Physical Linkage ◽  
Factor C ◽  
Redundant Functions ◽  
Mutant Cells

ABSTRACT CTF7/ECO1 is an essential yeast gene required for the establishment of sister chromatid cohesion. The findings that CTF7/ECO1, POL30 (PCNA), and CHL12/CTF18 (a replication factor C [RFC] homolog) genetically interact provided the first evidence that the processes of cohesion establishment and DNA replication are intimately coupled—a link now confirmed by other studies. To date, however, it is unknown how Ctf7p/Eco1p function is coupled to DNA replication or whether Ctf7p/Eco1p physically associates with any components of the DNA replication machinery. Here, we report that Ctf7p/Eco1p associates with proteins that perform partially redundant functions in DNA replication. Chl12p/Ctf18p combines with Rfc2p to Rfc5p to form one of three independent RFC complexes. By chromatographic methods, Ctf7p/Eco1p was found to associate with Chl12/Ctf18p and with Rfc2p, Rfc3p, Rfc4p, and Rfc5p. The association between Ctf7p/Eco1p and this RFC complex is biologically relevant in that (i) Ctf7p/Eco1p cosediments with Chl12p/Ctf18p in vivo and (ii) rfc5-1 mutant cells exhibit precocious sister separation. Previous studies revealed that Rfc1p or Rad24p associates with Rfc2p to Rfc5p to form two other RFC complexes independent of Ctf18p-RFC complexes. These Rfc1p-RFC and Rad24p-RFC complexes function in DNA replication or repair and DNA damage checkpoint pathways. Importantly, Ctf7p/Eco1p also associates with Rfc1p and Rad24p, suggesting that these RFC complexes also play critical roles in cohesion establishment. The associations between Ctf7p/Eco1p and RFC subunits provide novel evidence regarding the physical linkage between cohesion establishment and DNA replication. Furthermore, the association of Ctf7p/Eco1p with each of three RFC complexes supplies new insights into the functional redundancy of RFC complexes in cohesion establishment.

scholarly journals Phosphorylation of Serine 51 Regulates the Interaction of Human DNA Ligase I with Replication Factor C and Its Participation in DNA Replication and Repair

2012 ◽  
Vol 287 (44) ◽  
pp. 36711-36719 ◽  
Author(s):  
Zhimin Peng ◽  
Zhongping Liao ◽  
Barbara Dziegielewska ◽  
Yoshi Matsumoto ◽  
Stefani Thomas ◽  
...  
Keyword(s):  
Dna Replication ◽  
Dna Ligase ◽  
Replication Factor C ◽  
Replication Factor ◽  
Human Dna ◽  
Dna Ligase I ◽  
Dna Replication And Repair ◽  
Factor C

scholarly journals Identification of Regions within the Four Small Subunits of Human Replication Factor C Required for Complex Formation and DNA Replication

1997 ◽  
Vol 272 (15) ◽  
pp. 10065-10071 ◽  
Author(s):  
Frank Uhlmann ◽  
Emma Gibbs ◽  
Jinsong Cai ◽  
Mike O'Donnell ◽  
Jerard Hurwitz
Keyword(s):  
Dna Replication ◽  
Complex Formation ◽  
Replication Factor C ◽  
Replication Factor ◽  
Factor C

A plant homologue of 36 kDa subunit of replication factor C: molecular cloning and characterization

Plant Science ◽  
2001 ◽  
Vol 161 (1) ◽  
pp. 99-106 ◽  
Author(s):  
Tomoyuki Furukawa ◽  
Seisuke Kimura ◽  
Toyotaka Ishibashi ◽  
Junji Hashimoto ◽  
Kengo Sakaguchi
Keyword(s):  
Molecular Cloning ◽  
Replication Factor C ◽  
Replication Factor ◽  
Factor C ◽  
Plant Homologue

scholarly journals The C-terminal Domain (CTD) of Human DNA Glycosylase NEIL1 Is Required for Forming BERosome Repair Complex with DNA Replication Proteins at the Replicating Genome

2015 ◽  
Vol 290 (34) ◽  
pp. 20919-20933 ◽  
Author(s):  
Pavana M. Hegde ◽  
Arijit Dutta ◽  
Shiladitya Sengupta ◽  
Joy Mitra ◽  
Sanjay Adhikari ◽  
...  
Keyword(s):  
Dna Replication ◽  
Mammalian Cells ◽  
Dna Glycosylase ◽  
Nuclear Antigen ◽  
Replication Factor C ◽  
Replication Factor ◽  
Terminal Domain ◽  
Human Dna ◽  
Factor C

The human DNA glycosylase NEIL1 was recently demonstrated to initiate prereplicative base excision repair (BER) of oxidized bases in the replicating genome, thus preventing mutagenic replication. A significant fraction of NEIL1 in cells is present in large cellular complexes containing DNA replication and other repair proteins, as shown by gel filtration. However, how the interaction of NEIL1 affects its recruitment to the replication site for prereplicative repair was not investigated. Here, we show that NEIL1 binarily interacts with the proliferating cell nuclear antigen clamp loader replication factor C, DNA polymerase δ, and DNA ligase I in the absence of DNA via its non-conserved C-terminal domain (CTD); replication factor C interaction results in ∼8-fold stimulation of NEIL1 activity. Disruption of NEIL1 interactions within the BERosome complex, as observed for a NEIL1 deletion mutant (N311) lacking the CTD, not only inhibits complete BER in vitro but also prevents its chromatin association and reduced recruitment at replication foci in S phase cells. This suggests that the interaction of NEIL1 with replication and other BER proteins is required for efficient repair of the replicating genome. Consistently, the CTD polypeptide acts as a dominant negative inhibitor during in vitro repair, and its ectopic expression sensitizes human cells to reactive oxygen species. We conclude that multiple interactions among BER proteins lead to large complexes, which are critical for efficient BER in mammalian cells, and the CTD interaction could be targeted for enhancing drug/radiation sensitivity of tumor cells.

scholarly journals Chl12 (Ctf18) Forms a Novel Replication Factor C-Related Complex and Functions Redundantly with Rad24 in the DNA Replication Checkpoint Pathway

2001 ◽  
Vol 21 (17) ◽  
pp. 5838-5845 ◽  
Author(s):  
Takahiro Naiki ◽  
Tae Kondo ◽  
Daisuke Nakada ◽  
Kunihiro Matsumoto ◽  
Katsunori Sugimoto
Keyword(s):  
Dna Replication ◽  
Dna Damage Checkpoint ◽  
Replication Factor C ◽  
Replication Checkpoint ◽  
Replication Factor ◽  
Checkpoint Pathway ◽  
Dna Replication Checkpoint ◽  
Replication Block ◽  
Factor C ◽  
Related Complex

ABSTRACT RAD24 has been identified as a gene essential for the DNA damage checkpoint in budding yeast. Rad24 is structurally related to subunits of the replication factor C (RFC) complex, and forms an RFC-related complex with Rfc2, Rfc3, Rfc4, and Rfc5. Therad24Δ mutation enhances the defect ofrfc5-1 in the DNA replication block checkpoint, implicating RAD24 in this checkpoint.CHL12 (also called CTF18) encodes a protein that is structurally related to the Rad24 and RFC proteins. We show here that although neither chl12Δ norrad24Δ single mutants are defective, chl12Δ rad24Δ double mutants become defective in the replication block checkpoint. We also show that Chl12 interacts physically with Rfc2, Rfc3, Rfc4, and Rfc5 and forms an RFC-related complex which is distinct from the RFC and RAD24 complexes. Our results suggest that Chl12 forms a novel RFC-related complex and functions redundantly with Rad24 in the DNA replication block checkpoint.

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