Human PCNA Structure, Function, and Interactions

被引：239

作者：

Gonzalez-Magana, Amaia ^{[1
]}

Blanco, Francisco J. ^{[1
,2
]}

机构：

[1] CIC bioGUNE, Bizkaia Sci & Technol Pk,Bld 800, Derio 48160, Bizkaia, Spain

[2] Basque Fdn Sci, Ikerbasque, Maria Diaz Haro 3,6 Solairua, Bilbao 48013, Bizkaia, Spain

来源：

BIOMOLECULES | 2020年 / 10卷 / 04期

关键词：

PCNA; structure; protein interactions; DNA sliding; molecular recognition; DNA replication; DNA repair; CELL NUCLEAR ANTIGEN; CRYSTAL-STRUCTURE; PIP-BOX; TYROSINE PHOSPHORYLATION; DNA-REPLICATION; SLIDING CLAMP; IN-VITRO; PROTEIN; COMPLEX; UBIQUITINATION;

D O I：

10.3390/biom10040570

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Proliferating cell nuclear antigen (PCNA) is an essential factor inDNAreplication 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 ffi 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.

引用

页数：19

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