Human PCNA Structure, Function and Interactions

Proliferating cell nuclear antigen (PCNA) is an essential factor in DNA replication and repair. It forms a homotrimeric ring that embraces the DNA and slides along it, anchoring DNA polymerases and other DNA editing enzymes. It also interacts with regulatory proteins through a sequence motif known a...

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Bibliographic Details
Published in:Biomolecules (Basel, Switzerland) Switzerland), 2020-04, Vol.10 (4), p.570
Main Authors: González-Magaña, Amaia, Blanco, Francisco J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antigens
Cell cycle
Crystal structure
Deoxyribonucleic acid
DNA
DNA biosynthesis
DNA repair
DNA replication
DNA sliding
DNA-directed DNA polymerase
E coli
Humans
molecular recognition
NMR
Nuclear magnetic resonance
Nucleotide sequence
PCNA
Post-translation
Proliferating cell nuclear antigen
Proliferating Cell Nuclear Antigen - chemistry
Proliferating Cell Nuclear Antigen - metabolism
Protein Binding
protein interactions
Proteins
Regulatory proteins
Regulatory sequences
Replication
Review
structure
Structure-function relationships
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Summary:Proliferating cell nuclear antigen (PCNA) is an essential factor in DNA replication and repair. It forms a homotrimeric ring that embraces the DNA and slides along it, anchoring DNA polymerases and other DNA editing enzymes. It also interacts with regulatory proteins through a sequence motif known as PCNA Interacting Protein box (PIP-box). We here review the latest contributions to knowledge regarding the structure-function relationships in human PCNA, particularly the mechanism of sliding, and of the molecular recognition of canonical and non-canonical PIP motifs. The unique binding mode of the oncogene p15 is described in detail, and the implications of the recently discovered structure of PCNA bound to polymerase δ are discussed. The study of the post-translational modifications of PCNA and its partners may yield therapeutic opportunities in cancer treatment, in addition to illuminating the way PCNA coordinates the dynamic exchange of its many partners in DNA replication and repair.
ISSN:2218-273X
2218-273X
DOI:10.3390/biom10040570