Role of BRCA2 DNA-binding and C-terminal domain in its mobility and conformation in DNA repair.

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Tytuł:: Role of BRCA2 DNA-binding and C-terminal domain in its mobility and conformation in DNA repair.
Autorzy:: Paul MW; Department of Molecular Genetics, Oncode Institute, Erasmus MC Cancer Institute, Erasmus University Medical Center, Rotterdam, Netherlands.
Sidhu A; Department of Molecular Genetics, Oncode Institute, Erasmus MC Cancer Institute, Erasmus University Medical Center, Rotterdam, Netherlands.; Department of Radiation Oncology, Erasmus University Medical Center, Rotterdam, Netherlands.
Liang Y; Department of Molecular Genetics, Oncode Institute, Erasmus MC Cancer Institute, Erasmus University Medical Center, Rotterdam, Netherlands.
van Rossum-Fikkert SE; Department of Molecular Genetics, Oncode Institute, Erasmus MC Cancer Institute, Erasmus University Medical Center, Rotterdam, Netherlands.; Department of Radiation Oncology, Erasmus University Medical Center, Rotterdam, Netherlands.
Odijk H; Department of Molecular Genetics, Oncode Institute, Erasmus MC Cancer Institute, Erasmus University Medical Center, Rotterdam, Netherlands.
Zelensky AN; Department of Molecular Genetics, Oncode Institute, Erasmus MC Cancer Institute, Erasmus University Medical Center, Rotterdam, Netherlands.
Kanaar R; Department of Molecular Genetics, Oncode Institute, Erasmus MC Cancer Institute, Erasmus University Medical Center, Rotterdam, Netherlands.
Wyman C; Department of Molecular Genetics, Oncode Institute, Erasmus MC Cancer Institute, Erasmus University Medical Center, Rotterdam, Netherlands.; Department of Radiation Oncology, Erasmus University Medical Center, Rotterdam, Netherlands.
Źródło:: ELife [Elife] 2021 Jul 13; Vol. 10. Date of Electronic Publication: 2021 Jul 13.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
MeSH Terms:: DNA Repair*
Nucleic Acid Conformation*
BRCA2 Protein/*chemistry
BRCA2 Protein/*genetics
DNA-Binding Proteins/*chemistry
DNA-Binding Proteins/*genetics
Animals ; BRCA2 Protein/metabolism ; DNA/chemistry ; DNA/metabolism ; DNA Replication ; DNA-Binding Proteins/metabolism ; Homologous Recombination ; Humans ; Mice ; Mouse Embryonic Stem Cells ; Rad51 Recombinase/genetics ; Rad51 Recombinase/metabolism ; Single Molecule Imaging
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Contributed Indexing:: Keywords: BRCA2; DNA repair; biochemistry; cell biology; chemical biology; homologous recombination; human; mouse; nuclear foci; scanning force microscopy; single-molecule microscopy
Substance Nomenclature:: 0 (BRCA2 Protein)
0 (BRCA2 protein, human)
0 (DNA-Binding Proteins)
9007-49-2 (DNA)
EC 2.7.7.- (Rad51 Recombinase)
Entry Date(s):: Date Created: 20210713 Date Completed: 20211028 Latest Revision: 20240403
Update Code:: 20240403
PubMed Central ID:: PMC8324294
DOI:: 10.7554/eLife.67926
PMID:: 34254584
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Breast cancer type two susceptibility protein (BRCA2) is an essential protein in genome maintenance, homologous recombination (HR), and replication fork protection. Its function includes multiple interaction partners and requires timely localization to relevant sites in the nucleus. We investigated the importance of the highly conserved DNA-binding domain (DBD) and C-terminal domain (CTD) of BRCA2. We generated BRCA2 variants missing one or both domains in mouse embryonic stem (ES) cells and defined their contribution in HR function and dynamic localization in the nucleus, by single-particle tracking of BRCA2 mobility. Changes in molecular architecture of BRCA2 induced by binding partners of purified BRCA2 were determined by scanning force microscopy. BRCA2 mobility and DNA-damage-induced increase in the immobile fraction were largely unaffected by C-terminal deletions. The purified proteins missing CTD and/or DBD were defective in architectural changes correlating with reduced HR function in cells. These results emphasize BRCA2 activity at sites of damage beyond promoting RAD51 delivery.
Competing Interests: MP, AS, YL, Sv, HO, AZ, RK, CW No competing interests declared
(© 2021, Paul et al.)

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