Unknown

Dataset Information

0

Intricate SUMO-based control of the homologous recombination machinery.


ABSTRACT: The homologous recombination (HR) machinery plays multiple roles in genome maintenance. Best studied in the context of DNA double-stranded break (DSB) repair, recombination enzymes can cleave, pair, and unwind DNA molecules, and collaborate with regulatory proteins to execute multiple DNA processing steps before generating specific repair products. HR proteins also help to cope with problems arising from DNA replication, modulating impaired replication forks or filling DNA gaps. Given these important roles, it is not surprising that each HR step is subject to complex regulation to adjust repair efficiency and outcomes as well as to limit toxic intermediates. Recent studies have revealed intricate regulation of all steps of HR by the protein modifier SUMO, which has been increasingly recognized for its broad influence in nuclear functions. This review aims to connect established roles of SUMO with its newly identified effects on recombinational repair and stimulate further thought on many unanswered questions.

SUBMITTER: Dhingra N 

PROVIDER: S-EPMC6771382 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Intricate SUMO-based control of the homologous recombination machinery.

Dhingra Nalini N   Zhao Xiaolan X  

Genes & development 20191001 19-20


The homologous recombination (HR) machinery plays multiple roles in genome maintenance. Best studied in the context of DNA double-stranded break (DSB) repair, recombination enzymes can cleave, pair, and unwind DNA molecules, and collaborate with regulatory proteins to execute multiple DNA processing steps before generating specific repair products. HR proteins also help to cope with problems arising from DNA replication, modulating impaired replication forks or filling DNA gaps. Given these impo  ...[more]

Similar Datasets

| S-EPMC3679537 | biostudies-literature
| S-EPMC6771392 | biostudies-literature
| S-EPMC5599617 | biostudies-literature
| S-EPMC3203602 | biostudies-literature
| S-EPMC2635538 | biostudies-literature
| S-EPMC2642740 | biostudies-literature
| S-EPMC10928375 | biostudies-literature
| S-EPMC3855272 | biostudies-literature
| S-EPMC5571030 | biostudies-literature
| S-EPMC6957567 | biostudies-literature