scholarly journals Inactivating pentapeptide insertions in the fission yeast replication factor C subunit Rfc2 cluster near the ATP-binding site and arginine finger motif

FEBS Journal ◽  
2009 ◽  
Vol 276 (17) ◽  
pp. 4803-4813 ◽  
Author(s):  
Fiona C. Gray ◽  
Kathryn A. Whitehead ◽  
Stuart A. MacNeill
Keyword(s):  
Binding Site ◽  
Fission Yeast ◽  
Atp Binding ◽  
Replication Factor C ◽  
Atp Binding Site ◽  
Replication Factor ◽  
C Subunit ◽  
Factor C ◽  
Arginine Finger

scholarly journals Cloning, expression, and chromosomal localization of the 140-kilodalton subunit of replication factor C from mice and humans.

1994 ◽  
Vol 14 (3) ◽  
pp. 1626-1634 ◽  
Author(s):  
B Luckow ◽  
F Bunz ◽  
B Stillman ◽  
P Lichter ◽  
G Schütz
Keyword(s):  
Amino Acids ◽  
Molecular Mass ◽  
Binding Site ◽  
Peptide Sequence ◽  
Atp Binding ◽  
Sequence Information ◽  
Replication Factor C ◽  
Atp Binding Site ◽  
Replication Factor ◽  
Factor C

We have isolated a full-length mouse cDNA encoding a lysine-rich protein of 1,131 amino acids with a calculated molecular mass of 126 kDa. The protein binds in a sequence-unspecific manner to DNA, is localized exclusively in the nucleus, and contains a putative ATP binding site and a stretch of 80 amino acids with homology to the carboxy terminus of prokaryotic DNA ligases. On the basis of the following facts, we conclude that the isolated cDNA encodes the 140-kDa subunit of mouse replication factor C (mRFC140). (i) The sequence around the ATP binding site shows significant homology to three small subunits of human replication factor C. (ii) Polyclonal antibodies raised against the protein encoded by this cDNA cross-react with the 140-kDa subunit of purified human replication factor C (hRFC140) and recognize in mouse cell extracts an authentic protein with an apparent molecular mass of 130 kDa. (iii) Sequence comparison with a human cDNA isolated by using tryptic peptide sequence information from purified hRFC140 revealed 83% identity of the encoded proteins. The mRFC140 gene is ubiquitously expressed, and two mRNAs approximately 5.0 and 4.5 kb long have been detected. The gene was mapped by in situ hybridization to mouse chromosome 5, and its human homolog was mapped to chromosome 4 (p13-p14).

scholarly journals A genetic analysis of the 63E-64A genomic region of Drosophila melanogaster: identification of mutations in a replication factor C subunit.

Genetics ◽  
1995 ◽  
Vol 139 (4) ◽  
pp. 1701-1709 ◽  
Author(s):  
S D Harrison ◽  
N Solomon ◽  
G M Rubin
Keyword(s):  
Complementation Group ◽  
Genomic Region ◽  
Replication Factor C ◽  
Group 13 ◽  
Multiple Alleles ◽  
Replication Factor ◽  
Lethal Mutations ◽  
C Subunit ◽  
Complementation Groups ◽  
Factor C

Abstract We have performed an F2 genetic screen to identify lethal mutations within the 63E-64A genomic region. We have isolated 122 mutations in 20 different complementation groups. Of these groups, 16 are represented by multiple alleles. We have also established that the Rop and Ras2 genes are located within the 63E-64A genomic domain at 64A10,11. We have sequenced 10.2 kb of DNA surrounding this gene pair and find that in addition to Rop and Ras2 there is another gene located within this DNA sequence. The gene product, which we have named Rfc40, shows 68% identity to the 40-kDa subunit of replication factor C. We find that the members of one complementation group (13 alleles) derived from our screen correspond to mutations in the Rop gene, whereas the members of another (five alleles) correspond to mutations in the Rfc40 gene. In addition we have isolated 11 new mutant alleles of the disembodied gene.

scholarly journals MicroRNA‑744‑5p inhibits glioblastoma malignancy by suppressing replication factor C subunit 2

2021 ◽  
Vol 22 (2) ◽  
Author(s):  
Fei Fan ◽  
Dongxiao Yao ◽  
Pengfei Yan ◽  
Xiaobing Jiang ◽  
Jie Hu
Keyword(s):  
Replication Factor C ◽  
Replication Factor ◽  
C Subunit ◽  
Factor C

scholarly journals Forkhead box O1 targeting replication factor C subunit 2 expression promotes glioma temozolomide resistance and survival

2021 ◽  
Vol 9 (8) ◽  
pp. 692-692
Author(s):  
Xingsheng Qiu ◽  
Guifeng Tan ◽  
Hao Wen ◽  
Lian Lian ◽  
Songhua Xiao
Keyword(s):  
Replication Factor C ◽  
Replication Factor ◽  
Forkhead Box ◽  
C Subunit ◽  
Factor C

scholarly journals Plasmodium falciparum replication factor C subunit 1 is involved in genotoxic stress response

2020 ◽  
Author(s):  
Omar Sheriff ◽  
Aniweh Yaw ◽  
Soak Kuan Lai ◽  
hooi linn loo ◽  
Siu Kwan Sze ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Stress Response ◽  
Genotoxic Stress ◽  
Replication Factor C ◽  
Replication Factor ◽  
C Subunit ◽  
Factor C

scholarly journals Fission Yeast Cdc24 Is a Replication Factor C- and Proliferating Cell Nuclear Antigen-Interacting Factor Essential for S-Phase Completion

1999 ◽  
Vol 19 (2) ◽  
pp. 1038-1048 ◽  
Author(s):  
Hiroyuki Tanaka ◽  
Koichi Tanaka ◽  
Hiroshi Murakami ◽  
Hiroto Okayama
Keyword(s):  
Dna Replication ◽  
Fission Yeast ◽  
Proliferating Cell Nuclear Antigen ◽  
Large Subunit ◽  
Nuclear Antigen ◽  
Temperature Sensitive ◽  
Replication Factor C ◽  
Replication Factor ◽  
Factor C ◽  
Proliferating Cell

ABSTRACT At the nonpermissive temperature the fission yeastcdc24-M38 mutant arrests in the cell cycle with incomplete DNA replication as indicated by pulsed-field gel electrophoresis. Thecdc24 + gene encodes a 501-amino-acid protein with no significant homology to any known proteins. The temperature-sensitive cdc24 mutant is effectively rescued by pcn1 +, rfc1 + (a fission yeast homologue of RFC1), andhhp1 +, which encode the proliferating cell nuclear antigen (PCNA), the large subunit of replication factor C (RFC), and a casein kinase I involved in DNA damage repair, respectively. The Cdc24 protein binds PCNA and RFC1 in vivo, and the domains essential for Cdc24 function and for RFC1 and PCNA binding colocalize in the N-terminal two-thirds of the molecule. In addition,cdc24 + genetically interacts with the gene encoding the catalytic subunit of DNA polymerase ɛ, which is stimulated by PCNA and RFC, and with those encoding the fission yeast counterparts of Mcm2, Mcm4, and Mcm10. These results indicate that Cdc24 is an RFC- and PCNA-interacting factor required for DNA replication and might serve as a target for regulation.

New Mechanistic Insight on the PIM-1 Kinase Inhibitor AZD1208 Using Multidrug Resistant Human Erythroleukemia Cell Lines and Molecular Docking Simulations

2019 ◽  
Vol 19 (11) ◽  
pp. 914-926 ◽  
Author(s):  
Maiara Bernardes Marques ◽  
Michael González-Durruthy ◽  
Bruna Félix da Silva Nornberg ◽  
Bruno Rodrigues Oliveira ◽  
Daniela Volcan Almeida ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Binding Site ◽  
Cell Lines ◽  
Chemotherapeutic Agents ◽  
Atp Binding ◽  
Human Leukemia ◽  
Atp Binding Site ◽  
Mechanistic Insight ◽  
Multiple Drugs

Background:PIM-1 is a kinase which has been related to the oncogenic processes like cell survival, proliferation, and multidrug resistance (MDR). This kinase is known for its ability to phosphorylate the main extrusion pump (ABCB1) related to the MDR phenotype.Objective:In the present work, we tested a new mechanistic insight on the AZD1208 (PIM-1 specific inhibitor) under interaction with chemotherapy agents such as Daunorubicin (DNR) and Vincristine (VCR).Materials and Methods:In order to verify a potential cytotoxic effect based on pharmacological synergism, two MDR cell lines were used: Lucena (resistant to VCR) and FEPS (resistant to DNR), both derived from the K562 non-MDR cell line, by MTT analyses. The activity of Pgp was ascertained by measuring accumulation and the directional flux of Rh123. Furthermore, we performed a molecular docking simulation to delve into the molecular mechanism of PIM-1 alone, and combined with chemotherapeutic agents (VCR and DNR).Results:Our in vitro results have shown that AZD1208 alone decreases cell viability of MDR cells. However, co-exposure of AZD1208 and DNR or VCR reverses this effect. When we analyzed the ABCB1 activity AZD1208 alone was not able to affect the pump extrusion. Differently, co-exposure of AZD1208 and DNR or VCR impaired ABCB1 activity, which could be explained by compensatory expression of abcb1 or other extrusion pumps not analyzed here. Docking analysis showed that AZD1208 is capable of performing hydrophobic interactions with PIM-1 ATP- binding-site residues with stronger interaction-based negative free energy (FEB, kcal/mol) than the ATP itself, mimicking an ATP-competitive inhibitory pattern of interaction. On the same way, VCR and DNR may theoretically interact at the same biophysical environment of AZD1208 and also compete with ATP by the PIM-1 active site. These evidences suggest that AZD1208 may induce pharmacodynamic interaction with VCR and DNR, weakening its cytotoxic potential in the ATP-binding site from PIM-1 observed in the in vitro experiments.Conclusion:Finally, the current results could have a pre-clinical relevance potential in the rational polypharmacology strategies to prevent multiple-drugs resistance in human leukemia cancer therapy.

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