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ATP5O — PCNA

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Intact Interaction: Complex of 306 proteins (association, pull down) Komarova et al., Mol Cell Proteomics 2011
• IRef Intact Interaction: Complex of 156 proteins (association, anti tag coimmunoprecipitation) Lau et al., Cell 2012

Text-mined interactions from Literome

Henneke et al., J Mol Biol 2002 : The Pab proliferating cell nuclear antigen ( PCNA ) activated the PabRFC complex in a DNA dependent manner, but the PabRFC-small ATPase activity was neither DNA dependent nor PCNA dependent ... Finally, ( i ) the PabRFC-large fraction cross reacted with anti-human-RFC PCNA binding domain antibody, corroborating the conservation of the protein sequence, ( ii ) the human PCNA stimulated the PabRFC complex ATPase activity in a DNA dependent way and ( iii ) the PabRFC complex could load human PCNA onto primed single stranded circular DNA, suggesting that the PCNA binding domain of RFC has been functionally conserved during evolution
Shiomi et al., Genes Cells 2004 : The purified Chl12-RFC complex is structurally indistinguishable from RFC, as shown by electron microscopy, and it exhibits DNA stimulated ATPase activity that is further enhanced by PCNA , and by DNA binding activity on specific primer/template DNA structures
Bagewadi et al., J Virol 2004 : The site-specific nicking closing activity and the ATPase function of IMYMV Rep were impaired by PCNA
Yoder et al., J Biol Chem 1991 : Calf thymus PCNA also stimulated the ATPase activity of yeast RF-C and participated in holoenzyme formation with DNA polymerase delta
Tsurimoto et al., Proc Natl Acad Sci U S A 1990 : Furthermore, PCNA stimulated the RF-C ATPase activity and is, therefore, analogous to the phage T4 gene 45 protein, which stimulates the ATPase function of the gene 44/62 protein complex
McNally et al., BMC structural biology 2010 : We show that simultaneous mutation of Lys 20, Lys 77, Arg 80, and Arg 149, which interact with DNA in the RFC-PCNA-DNA model, compromises the ability of yeast PCNA to stimulate the DNA dependent ATPase activity of RFC when the DNA is long enough to extend through the clamp ... Fluorescence anisotropy binding experiments show that the inability of the mutant clamp proteins to stimulate RFC ATPase activity is likely caused by reduction in the affinity of the RFC-PCNA complex for DNA
Oku et al., Genes Cells 1998 : Competition between p21 and pol delta or RFC for binding to PCNA results in efficient inhibition of its stimulation of pol delta DNA synthesis and RFC ATPase but not of PCNA loading on DNA by RFC