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Article ; Online: Branch Migration Activity of Rad54 Protein.

Mazina, Olga M / Mazin, Alexander V

Methods in molecular biology (Clifton, N.J.)

2020 Volume 2153, Page(s) 145–167

Abstract: Rad54 is a eukaryotic protein that plays an important role in homologous recombination. Rad54, a member of the Swi2/Snf2 family, binds to Holliday junctions with high specificity and promotes their branch migration in an ATP hydrolysis-dependent manner. ... ...

Abstract	Rad54 is a eukaryotic protein that plays an important role in homologous recombination. Rad54, a member of the Swi2/Snf2 family, binds to Holliday junctions with high specificity and promotes their branch migration in an ATP hydrolysis-dependent manner. Here we describe the methods our laboratory used to characterize the branch migration activity of Rad54. These assays are applicable for other branch migration proteins regardless of whether they have canonical helicase activity or not.
MeSH term(s)	Adenosine Triphosphate/metabolism ; DNA/chemistry ; DNA/metabolism ; DNA Breaks, Double-Stranded ; DNA Helicases/metabolism ; DNA-Binding Proteins/metabolism ; Electrophoresis, Polyacrylamide Gel ; Humans ; Hydrolysis ; Meiosis
Chemical Substances	DNA-Binding Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; DNA (9007-49-2) ; DNA Helicases (EC 3.6.4.-) ; RAD54L protein, human (EC 3.6.4.-)
Language	English
Publishing date	2020-08-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-0644-5_11
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Article ; Online: The function of RAD52 N-terminal domain is essential for viability of BRCA-deficient cells.

Hanamshet, Kritika / Mazin, Alexander V

Nucleic acids research

2020 Volume 48, Issue 22, Page(s) 12778–12791

Abstract: RAD52 is a member of the homologous recombination pathway that is important for survival of BRCA-deficient cells. Inhibition of RAD52 leads to lethality in BRCA-deficient cells. However, the exact mechanism of how RAD52 contributes to viability of BRCA- ... ...

Abstract	RAD52 is a member of the homologous recombination pathway that is important for survival of BRCA-deficient cells. Inhibition of RAD52 leads to lethality in BRCA-deficient cells. However, the exact mechanism of how RAD52 contributes to viability of BRCA-deficient cells remains unknown. Two major activities of RAD52 were previously identified: DNA or RNA pairing, which includes DNA/RNA annealing and strand exchange, and mediator, which is to assist RAD51 loading on RPA-covered ssDNA. Here, we report that the N-terminal domain (NTD) of RAD52 devoid of the potential mediator function is essential for maintaining viability of BRCA-deficient cells owing to its ability to promote DNA/RNA pairing. We show that RAD52 NTD forms nuclear foci upon DNA damage in BRCA-deficient human cells and promotes DNA double-strand break repair through two pathways: homology-directed repair (HDR) and single-strand annealing (SSA). Furthermore, we show that mutations in the RAD52 NTD that disrupt these activities fail to maintain viability of BRCA-deficient cells.
MeSH term(s)	BRCA1 Protein/genetics ; BRCA2 Protein/genetics ; Breast Neoplasms/genetics ; Breast Neoplasms/pathology ; Cell Line, Tumor ; DNA Damage/genetics ; DNA, Single-Stranded/genetics ; Female ; Gene Expression Regulation, Neoplastic/genetics ; Gene Knockout Techniques ; Humans ; Mutation/genetics ; Protein Binding/genetics ; Rad51 Recombinase/genetics ; Rad52 DNA Repair and Recombination Protein/genetics ; Recombinational DNA Repair/genetics
Chemical Substances	BRCA1 Protein ; BRCA1 protein, human ; BRCA2 Protein ; BRCA2 protein, human ; DNA, Single-Stranded ; RAD52 protein, human ; Rad52 DNA Repair and Recombination Protein ; Rad51 Recombinase (EC 2.7.7.-)
Language	English
Publishing date	2020-12-04
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkaa1145
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Zs.A 1067: Show issues

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Article ; Online: New RAD51 Inhibitors to Target Homologous Recombination in Human Cells.

Shkundina, Irina S / Gall, Alexander A / Dick, Alexej / Cocklin, Simon / Mazin, Alexander V

Genes

2021 Volume 12, Issue 6

Abstract: Targeting DNA repair proteins with small-molecule inhibitors became a proven anti-cancer strategy. Previously, we identified an inhibitor of a major protein of homologous recombination (HR) RAD51, named B02. B02 inhibited HR in human cells and sensitized ...

Abstract	Targeting DNA repair proteins with small-molecule inhibitors became a proven anti-cancer strategy. Previously, we identified an inhibitor of a major protein of homologous recombination (HR) RAD51, named B02. B02 inhibited HR in human cells and sensitized them to chemotherapeutic drugs
Language	English
Publishing date	2021-06-16
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2527218-4
ISSN	2073-4425 ; 2073-4425
ISSN (online)	2073-4425
ISSN	2073-4425
DOI	10.3390/genes12060920
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Article ; Online: Reconstituting the 4-Strand DNA Strand Exchange.

Mazina, Olga M / Mazin, Alexander V

Methods in enzymology

2018 Volume 600, Page(s) 285–305

Abstract: Proteins of the Rad51 family play a key role in homologous recombination by carrying out DNA strand exchange. Here, we present the methodology and the protocols for the 4-strand exchange between gapped circular DNA and homologous linear duplex DNA ... ...

Abstract	Proteins of the Rad51 family play a key role in homologous recombination by carrying out DNA strand exchange. Here, we present the methodology and the protocols for the 4-strand exchange between gapped circular DNA and homologous linear duplex DNA promoted by human Rad51 and Escherichia coli RecA orthologs. This reaction includes formation of joint molecules and their extension by branch migration in a polar manner. The presented methodology may be used for reconstitution of the medial-to-late stages of homologous recombination in vitro as well as for investigation of the mechanisms of branch migration by helicase-like proteins, e.g., Rad54, BLM, or RecQ1.
MeSH term(s)	DNA, Circular/chemistry ; DNA, Circular/metabolism ; Escherichia coli Proteins/metabolism ; Isotope Labeling/instrumentation ; Isotope Labeling/methods ; Nucleic Acid Heteroduplexes/chemistry ; Nucleic Acid Heteroduplexes/metabolism ; Phosphorus Radioisotopes/chemistry ; Rad51 Recombinase/metabolism ; Rec A Recombinases/metabolism ; Recombinational DNA Repair ; Staining and Labeling/instrumentation ; Staining and Labeling/methods
Chemical Substances	DNA, Circular ; Escherichia coli Proteins ; Nucleic Acid Heteroduplexes ; Phosphorus Radioisotopes ; Phosphorus-32 (690284A407) ; RAD51 protein, human (EC 2.7.7.-) ; Rad51 Recombinase (EC 2.7.7.-) ; Rec A Recombinases (EC 2.7.7.-)
Language	English
Publishing date	2018-02-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1557-7988 ; 0076-6879
ISSN (online)	1557-7988
ISSN	0076-6879
DOI	10.1016/bs.mie.2017.11.013
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Article ; Online: Multiscale spatial mapping of cell populations across anatomical sites in healthy human skin and basal cell carcinoma.

Ganier, Clarisse / Mazin, Pavel / Herrera-Oropeza, Gabriel / Du-Harpur, Xinyi / Blakeley, Matthew / Gabriel, Jeyrroy / Predeus, Alexander V / Cakir, Batuhan / Prete, Martin / Harun, Nasrat / Darrigrand, Jean-Francois / Haiser, Alexander / Wyles, Saranya / Shaw, Tanya / Teichmann, Sarah A / Haniffa, Muzlifah / Watt, Fiona M / Lynch, Magnus D

Proceedings of the National Academy of Sciences of the United States of America

2024 Volume 121, Issue 2, Page(s) e2313326120

Abstract: Our understanding of how human skin cells differ according to anatomical site and tumour formation is limited. To address this, we have created a multiscale spatial atlas of healthy skin and basal cell carcinoma (BCC), incorporating in vivo optical ... ...

Abstract	Our understanding of how human skin cells differ according to anatomical site and tumour formation is limited. To address this, we have created a multiscale spatial atlas of healthy skin and basal cell carcinoma (BCC), incorporating in vivo optical coherence tomography, single-cell RNA sequencing, spatial global transcriptional profiling, and in situ sequencing. Computational spatial deconvolution and projection revealed the localisation of distinct cell populations to specific tissue contexts. Although cell populations were conserved between healthy anatomical sites and in BCC, mesenchymal cell populations including fibroblasts and pericytes retained signatures of developmental origin. Spatial profiling and in silico lineage tracing support a hair follicle origin for BCC and demonstrate that cancer-associated fibroblasts are an expansion of a
MeSH term(s)	Humans ; Carcinoma, Basal Cell ; Skin Neoplasms/pathology ; Skin/pathology ; Hair Follicle
Language	English
Publishing date	2024-01-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2313326120
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Article: New RAD51 Inhibitors to Target Homologous Recombination in Human Cells

Shkundina, Irina S. / Gall, Alexander A. / Dick, Alexej / Cocklin, Simon / Mazin, Alexander V.

Genes. 2021 June 16, v. 12, no. 6

2021

Abstract	Targeting DNA repair proteins with small-molecule inhibitors became a proven anti-cancer strategy. Previously, we identified an inhibitor of a major protein of homologous recombination (HR) RAD51, named B02. B02 inhibited HR in human cells and sensitized them to chemotherapeutic drugs in vitro and in vivo. Here, using a medicinal chemistry approach, we aimed to improve the potency of B02. We identified the B02 analog, B02-isomer, which inhibits HR in human cells with significantly higher efficiency. We also show that B02-iso sensitizes triple-negative breast cancer MDA-MB-231 cells to the PARP inhibitor (PARPi) olaparib.
Keywords	DNA repair ; breast neoplasms ; chemistry ; drug therapy ; homologous recombination ; humans
Language	English
Dates of publication	2021-0616
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2527218-4
ISSN	2073-4425
ISSN	2073-4425
DOI	10.3390/genes12060920
Database	NAL-Catalogue (AGRICOLA)

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Article: RAD52: Paradigm of Synthetic Lethality and New Developments.

Rossi, Matthew J / DiDomenico, Sarah F / Patel, Mikir / Mazin, Alexander V

Frontiers in genetics

2021 Volume 12, Page(s) 780293

Abstract: DNA double-strand breaks and inter-strand cross-links are the most harmful types of DNA damage that cause genomic instability that lead to cancer development. The highest fidelity pathway for repairing damaged double-stranded DNA is termed Homologous ... ...

Abstract	DNA double-strand breaks and inter-strand cross-links are the most harmful types of DNA damage that cause genomic instability that lead to cancer development. The highest fidelity pathway for repairing damaged double-stranded DNA is termed Homologous recombination (HR). Rad52 is one of the key HR proteins in eukaryotes. Although it is critical for most DNA repair and recombination events in yeast, knockouts of mammalian RAD52 lack any discernable phenotypes. As a consequence, mammalian RAD52 has been long overlooked. That is changing now, as recent work has shown RAD52 to be critical for backup DNA repair pathways in HR-deficient cancer cells. Novel findings have shed light on RAD52's biochemical activities. RAD52 promotes DNA pairing (D-loop formation), single-strand DNA and DNA:RNA annealing, and inverse strand exchange. These activities contribute to its multiple roles in DNA damage repair including HR, single-strand annealing, break-induced replication, and RNA-mediated repair of DNA. The contributions of RAD52 that are essential to the viability of HR-deficient cancer cells are currently under investigation. These new findings make RAD52 an attractive target for the development of anti-cancer therapies against BRCA-deficient cancers.
Language	English
Publishing date	2021-11-23
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2606823-0
ISSN	1664-8021
ISSN	1664-8021
DOI	10.3389/fgene.2021.780293
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Article ; Online: Structural insights into BCDX2 complex function in homologous recombination.

Rawal, Yashpal / Jia, Lijia / Meir, Aviv / Zhou, Shuo / Kaur, Hardeep / Ruben, Eliza A / Kwon, Youngho / Bernstein, Kara A / Jasin, Maria / Taylor, Alexander B / Burma, Sandeep / Hromas, Robert / Mazin, Alexander V / Zhao, Weixing / Zhou, Daohong / Wasmuth, Elizabeth V / Greene, Eric C / Sung, Patrick / Olsen, Shaun K

Nature

2023 Volume 619, Issue 7970, Page(s) 640–649

Abstract: Homologous recombination (HR) fulfils a pivotal role in the repair of DNA double-strand breaks and collapsed replication ... ...

Abstract	Homologous recombination (HR) fulfils a pivotal role in the repair of DNA double-strand breaks and collapsed replication forks
MeSH term(s)	Humans ; Cryoelectron Microscopy ; DNA Replication ; DNA, Single-Stranded/chemistry ; DNA, Single-Stranded/genetics ; DNA, Single-Stranded/metabolism ; DNA, Single-Stranded/ultrastructure ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; DNA-Binding Proteins/ultrastructure ; Homologous Recombination ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/metabolism ; Multiprotein Complexes/ultrastructure ; Neoplasms/genetics ; Nucleoproteins/metabolism ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; Rad51 Recombinase/chemistry ; Rad51 Recombinase/metabolism ; Rad51 Recombinase/ultrastructure ; Substrate Specificity
Chemical Substances	DNA, Single-Stranded ; DNA-Binding Proteins ; Multiprotein Complexes ; Nucleoproteins ; Protein Subunits ; Rad51 Recombinase (EC 2.7.7.-) ; RAD51B protein, human ; RAD51C protein, human ; RAD51D protein, human ; XRCC2 protein, human
Language	English
Publishing date	2023-06-21
Publishing country	England
Document type	Journal Article
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-023-06219-w
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Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: A novel landscape of nuclear human CDK2 substrates revealed by in situ phosphorylation.

Chi, Yong / Carter, John H / Swanger, Jherek / Mazin, Alexander V / Moritz, Robert L / Clurman, Bruce E

Science advances

2020 Volume 6, Issue 16, Page(s) eaaz9899

Abstract: Cyclin-dependent kinase 2 (CDK2) controls cell division and is central to oncogenic signaling. We used an "in situ" approach to identify CDK2 substrates within nuclei isolated from cells expressing CDK2 engineered to use adenosine 5'-triphosphate analogs. ...

Abstract	Cyclin-dependent kinase 2 (CDK2) controls cell division and is central to oncogenic signaling. We used an "in situ" approach to identify CDK2 substrates within nuclei isolated from cells expressing CDK2 engineered to use adenosine 5'-triphosphate analogs. We identified 117 candidate substrates, ~40% of which are known CDK substrates. Previously unknown candidates were validated to be CDK2 substrates, including LSD1, DOT1L, and Rad54. The identification of many chromatin-associated proteins may have been facilitated by labeling conditions that preserved nuclear architecture and physiologic CDK2 regulation by endogenous cyclins. Candidate substrates include proteins that regulate histone modifications, chromatin, transcription, and RNA/DNA metabolism. Many of these proteins also coexist in multi-protein complexes, including epigenetic regulators, that may provide new links between cell division and other cellular processes mediated by CDK2. In situ phosphorylation thus revealed candidate substrates with a high validation rate and should be readily applicable to other nuclear kinases.
Language	English
Publishing date	2020-04-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.aaz9899
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Article ; Online: Targeting the homologous recombination pathway by small molecule modulators.

Huang, Fei / Mazin, Alexander V

Bioorganic & medicinal chemistry letters

2014 Volume 24, Issue 14, Page(s) 3006–3013

Abstract: During the last decade, the use of small molecule (MW <500 Da) compounds that modulate (inhibit or activate) important proteins of different biological pathways became widespread. Recently, the homologous recombination (HR) pathway emerged as a target ... ...

Abstract	During the last decade, the use of small molecule (MW <500 Da) compounds that modulate (inhibit or activate) important proteins of different biological pathways became widespread. Recently, the homologous recombination (HR) pathway emerged as a target for such modulators. Development of small molecule modulators pursues two distinct but not mutually exclusive purposes: to create a research tool to study the activities or functions of proteins of interest and to produce drugs targeting specific pathologies. Here, we review the progress of small molecule development in the area of HR.
MeSH term(s)	Animals ; Homologous Recombination/drug effects ; Humans ; Small Molecule Libraries/chemical synthesis ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/pharmacology
Chemical Substances	Small Molecule Libraries
Language	English
Publishing date	2014-05-06
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1063195-1
ISSN	1464-3405 ; 0960-894X
ISSN (online)	1464-3405
ISSN	0960-894X
DOI	10.1016/j.bmcl.2014.04.088
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Zs.A 3203: Show issues

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