A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification.

A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification. Research Abstract Details 

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A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification. Abstract Text:

Karen H Almeida,Robert W Sobol,

Base excision repair (BER) proteins act upon a significantly broad spectrum of DNA lesions that result from endogenous and exogenous sources. Multiple sub-pathways of BER (short-path or long-patch) and newly designated DNA repair pathways (e.g., SSBR and NIR) that utilize BER proteins complicate any comprehensive understanding of BER and its role in genome maintenance, chemotherapeutic response, neuro-degeneration, cancer or aging. Herein, we propose a unified model of BER, comprised of three functional processes: Lesion Recognition/Strand Scission, Gap Tailoring and DNA Synthesis/Ligation, each represented by one or more multi-protein complexes and coordinated via the XRCC1/DNA Ligase III and PARP1 scaffold proteins. BER therefore may be represented by a series of repair complexes that assemble at the site of the DNA lesion and mediates repair in a coordinated fashion involving protein-protein interactions that dictate subsequent steps or sub-pathway choice. Complex formation is influenced by post-translational protein modifications that arise from the cellular state or the DNA damage response, providing an increase in specificity and efficiency to the BER pathway. In this review, we have summarized the reported BER protein-protein interactions and protein post-translational modifications and discuss the impact on DNA repair capacity and complex formation.

A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification. Publishing Authors By Initials

KH Almeida,RW Sobol,

For similar genetic processes: gene expression regulation: protein modification, translational: protein processing, post-translational research abstracts see: genetic processes: gene expression regulation: protein modification, translational: protein processing, post-translational research

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A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification. Journal Published:

PUBLICATION TYPE: Review

Journal: DNA repair

VOLUME: 6

Page Numbers: 695-711

Journal Abbreviation:

ISSN: 1568-7864

DAY: 6

MONTH: 03

YEAR: 2007

A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101139138

A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification. Keywords Mesh Terms:

KEYWORDS: Protein Processing, Post-Translational

MESH TERMS: metabolism

Chemical & Substance for Abstract: A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification. Information

Substance Name: DNA Topoisomerases

Registry Number: EC 5.99.1.-

Grant and Affiliation Information for A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification.

AFFILIATION: Department of Physical Sciences, Rhode Island College, 600 Mt. Pleasant Avenue, Providence, RI 02908-1991, United States.

Country: Netherlands

AGENCY: United States NCRR

GRANT: P20 RR016457

ACRONYM: RR

MEDLINETA: DNA Repair (Amst)

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