OB-fold Families of Genome Guardians: A Universal Theme Constructed From the Small β-barrel Building Block

The maintenance of genome stability requires the coordinated actions of multiple proteins and protein complexes, that are collectively known as genome guardians. Within this broadly defined family is a subset of proteins that contain oligonucleotide/oligosaccharide-binding folds (OB-fold). While OB-...

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Bibliographic Details
Published inFrontiers in molecular biosciences Vol. 9; p. 784451
Main Author Bianco, Piero R
Format Journal Article
LanguageEnglish
Published Switzerland Frontiers Media S.A 11.02.2022
Subjects
genome guardian
MCM
Molecular Biosciences
OB-fold
PXXP
SBB family
SH3 domain
SBB family
SH3 domain
PXXP
MCM
genome guardian
BRCA2
OB-fold
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Summary:The maintenance of genome stability requires the coordinated actions of multiple proteins and protein complexes, that are collectively known as genome guardians. Within this broadly defined family is a subset of proteins that contain oligonucleotide/oligosaccharide-binding folds (OB-fold). While OB-folds are widely associated with binding to single-stranded DNA this view is no longer an accurate depiction of how these domains are utilized. Instead, the core of the OB-fold is modified and adapted to facilitate binding to a variety of DNA substrates (both single- and double-stranded), phospholipids, and proteins, as well as enabling catalytic function to a multi-subunit complex. The flexibility accompanied by distinctive oligomerization states and quaternary structures enables OB-fold genome guardians to maintain the integrity of the genome via a myriad of complex and dynamic, protein-protein; protein-DNA, and protein-lipid interactions in both prokaryotes and eukaryotes.
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This article was submitted to Structural Biology, a section of the journal Frontiers in Molecular Biosciences
Edited by: Nicholas Robinson, Lancaster University, United Kingdom
Reviewed by: Jason A. Stewart, University of South Carolina, United States
Andrei Alexandrescu, University of Connecticut, United States
ISSN:2296-889X
2296-889X
DOI:10.3389/fmolb.2022.784451