KAUST DepartmentBiological and Environmental Science and Engineering (BESE) Division
Center for Desert Agriculture
Laboratory of DNA Replication and Recombination
Online Publication Date2018-01-30
Print Publication Date2018
Permanent link to this recordhttp://hdl.handle.net/10754/627270
MetadataShow full item record
AbstractProliferating cell nuclear antigen (PCNA) consists of three identical monomers that topologically encircle double-stranded DNA. PCNA stimulates the processivity of DNA polymerase δ and, to a less extent, the intrinsically highly processive DNA polymerase ε. It also functions as a platform that recruits and coordinates the activities of a large number of DNA processing proteins. Emerging structural and biochemical studies suggest that the nature of PCNA-partner proteins interactions is complex. A hydrophobic groove at the front side of PCNA serves as a primary docking site for the consensus PIP box motifs present in many PCNA-binding partners. Sequences that immediately flank the PIP box motif or regions that are distant from it could also interact with the hydrophobic groove and other regions of PCNA. Posttranslational modifications on the backside of PCNA could add another dimension to its interaction with partner proteins. An encounter of PCNA with different DNA structures might also be involved in coordinating its interactions. Finally, the ability of PCNA to bind up to three proteins while topologically linked to DNA suggests that it would be a versatile toolbox in many different DNA processing reactions.
CitationOke M, Zaher MS, Hamdan SM (2018) PCNA Structure and Interactions with Partner Proteins. Molecular Life Sciences: 866–872. Available: http://dx.doi.org/10.1007/978-1-4614-1531-2_138.
JournalMolecular Life Sciences