Search results for RFC1

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Protein (2 results from a total of 2)

Identifier: R-HSA-68435
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: RFC1: P35251
Identifier: R-HSA-200737
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: SLC19A1: P41440

Reaction (5 results from a total of 5)

Identifier: R-HSA-9668902
Species: Homo sapiens
Compartment: nucleoplasm
The CTF18 complex, composed of RFC1 homolog CHTF18 (CTF18), CHTF8 (CTF8) and DSCC1 (DCC1) binds to RFC2, RFC3, RFC4 and RFC5 to form the evolutionarily conserved heteroheptameric CTF18-RFC complex (CTF18-RFC(7s)), in which the RFC1 subunit of the RFC complex is replaced with the CTF18 complex (Bermudez et al. 2003, Merkle et al. 2003). CHTF18 is able to form a heteropentameric CTF18-RFC complex (CTF18-RFC(5s)) with RFC2, RFC3, RFC4 and RFC5 in the absence of CHTF8 and DSCC1 (Bermudez et al. 2003, Shiomi et al. 2004).
Identifier: R-HSA-9668904
Species: Homo sapiens
Compartment: nucleoplasm
CHTF18 (CTF18), a homolog of the RFC complex subunit RFC1, binds to CHTF8 (CTF8) and DSCC1 (DCC1) to form the evolutionarily conserved CTF18 complex (Merkle et al. 2003, Bermudez et al. 2003). Formation of a heterodimer between DSCC1 and CHTF8 may precede formation of a heterotrimer (Bermudez et al. 2003).
Identifier: R-HSA-174452
Species: Homo sapiens
Compartment: nucleoplasm
Once the RNA-DNA primer is synthesized, replication factor C (RFC) initiates a reaction called "polymerase switching"; pol delta, the processive enzyme, replaces pol alpha, the priming enzyme. RFC binds to the 3'-end of the RNA-DNA primer on the Primosome, to displace the pol alpha primase complex. The binding of RFC triggers the binding of the primer recognition complex (Tsurimoto and Stillman 1991, Maga et al. 2000, Mossi et al. 2000). RFC is recruited to telomeres via interaction with 5'-phosphate ends of a telomere repeat sequence (Uchiumi et al. 1996, Uchiumi et al. 1999). In budding yeast, the alternative evolutionarily conserved RFC complex in which the RFC1 subunit is substituted with the CTF18 complex (composed of CHTF18, CHTF8 and DSCC1) plays a critical role in telomere maintenance (Hiraga et al. 2006, Gao et al. 2014). The CTF18-RFC complex is also implicated in telomere maintenance in fission yeast (Khair et al. 2010). It was shown that the human CTF18-RFC complex has a redundant function with the RFC pentamer in PCNA loading and DNA replication (Bermudez et al. 2003), but its role in human telomere maintenance has not been studied. Mouse CFT18 complex is necessary for proper development of germ cells (Berkowitz et al. 2012).
Identifier: R-HSA-69053
Species: Homo sapiens
Compartment: nucleoplasm
Once the RNA-DNA primer is synthesized, replication factor C (RFC) initiates a reaction called "polymerase switching"; pol delta, the processive enzyme, replaces pol alpha, the priming enzyme. RFC binds to the 3'-end of the RNA-DNA primer on the Primosome, to displace the pol alpha primase complex. The binding of RFC triggers the binding of the primer recognition complex (Tsurimoto and Stillman 1991, Maga et al. 2000, Mossi et al. 2000). RFC is recruited to telomeres via interaction with 5'-phosphate ends of a telomere repeat sequence (Uchiumi et al. 1996, Uchiumi et al. 1999). In budding yeast, the alternative evolutionarily conserved RFC complex in which the RFC1 subunit is substituted with the CTF18 complex (composed of CHTF18, CHTF8 and DSCC1) plays a critical role in telomere maintenance (Hiraga et al. 2006, Gao et al. 2014). The CTF18-RFC complex is also implicated in telomere maintenance in fission yeast (Khair et al. 2010). It was shown that the human CTF18-RFC complex has a redundant function with the RFC pentamer in PCNA loading and DNA replication (Bermudez et al. 2003), but its role in human telomere maintenance has not been studied. Mouse CFT18 complex is necessary for proper development of germ cells (Berkowitz et al. 2012).
Identifier: R-HSA-176101
Species: Homo sapiens
Compartment: nucleoplasm
The Rad17-RFC complex is involved in an early stage of the genotoxic stress response. The major function of the protein complex is to load the Rad9-Hus1-Rad1 (9-1-1) complex onto DNA at sites of damage and/or stalled replication forks. This reaction is conceptually similar to the loading of the PCNA sliding clamp onto DNA by RFC. The association of the Rad17-RFC complex with ssDNA or gapped or primed DNA is significantly stimulated by RPA, but not by the heterologous E. coli SSB. Loading of the human 9-1-1 complex onto such DNA templates is also strongly stimulated by cognate RPA, but not yeast RPA. Although Rad17 and Rad9 are substrates of the ATR kinase activity, loading of the Rad17 and 9-1-1 complexes onto DNA occurs independent of ATR.

The Rad17-RFC complex is a heteropentamer structurally similar to RFC. The complex contains the four smaller RFC subunits (Rfc2 [p37], Rfc3 [p36], Rfc4 [p40], and Rfc5 [p38]) and the 75 kDa Rad17 subunit in place of the Rfc1 [p140] subunit. The Rad17 complex contains a weak ATPase that is slightly stimulated by primed DNA. Along with binding the 9-1-1 complex and RPA, the Rad17-RFC complex interacts with human MCM7 protein. Each of these interactions is critical for Chk1 activation.

The Rad17 subunit is conserved evolutionarily with the protein showing 49% identity at the amino acid level with the S. pombe rad17 protein. Targeted deletion of the N-terminal region of mouse Rad17 leads to embryonic lethality, strongly suggesting that human Rad17 is also essential for long-term viability.

Rad17-RFC complex associates with DNA substrates containing ssDNA regions including gapped or primed DNA in an ATP-independent reaction. Loading of the Rad9-Hus1-Rad1 (9-1-1) complex occurs preferentially on DNA substrates containing a 5' recessed end. This contrasts with the loading of PCNA by RFC which preferentially occurs on DNA with 3' recessed ends.

Complex (1 results from a total of 1)

Identifier: R-HSA-176353
Species: Homo sapiens
Compartment: nucleoplasm
The Rad17-RFC complex is a heteropentamer structurally similar to RFC. The Rad17-RFC complex contains the four smaller RFC subunits (Rfc2 [p37], Rfc3 [p36], Rfc4 [p40], and Rfc5 [p38]) and the 75 kDa Rad17 subunit in place of the Rfc1 [p140] subunit. The Rad17 complex contains a weak ATPase that is poorly stimulated by primed DNA. Along with binding the 9-1-1 complex and RPA, the Rad17-RFC complex interacts with human MCM7 protein. Each of these interactions is critical for Chk1 activation.

The Rad17 subunit is conserved evolutionarily with the protein showing 49% identity at the amino acid level with the S. pombe rad17 protein. Targeted deletion of the N-terminal region of mouse Rad17 leads to embryonic lethality, strongly suggesting that human Rad17 is also essential for long-term viability.

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