Human RPA activates BLM’s bidirectional DNA unwinding from a nick

BLM is a multifunctional helicase that plays critical roles in maintaining genome stability. It processes distinct DNA substrates, but not nicked DNA, during many steps in DNA replication and repair. However, how BLM prepares itself for diverse functions remains elusive. Here, using a combined singl...

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Published in:	eLife Vol. 9
Main Authors:	Qin, Zhenheng, Bi, Lulu, Hou, Xi-Miao, Zhang, Siqi, Zhang, Xia, Lu, Ying, Li, Ming, Modesti, Mauro, Xi, Xu-Guang, Sun, Bo
Format:	Journal Article
Language:	English
Published:	England eLife Science Publications, Ltd 26.02.2020 eLife Sciences Publications Ltd eLife Sciences Publication eLife Sciences Publications, Ltd
Subjects:	BLM Cellular Biology Deoxyribonucleic acid DNA DNA biosynthesis DNA Breaks, Single-Stranded DNA damage DNA helicase DNA repair DNA replication DNA Topoisomerases, Type I - metabolism DNA unwinding DNA, Single-Stranded - metabolism Genomes Genomics helicase Life Sciences Microscopy Novels optical tweezers Proteins RecQ Helicases - metabolism Replication protein A Replication Protein A - metabolism RPA single molecule Structural Biology and Molecular Biophysics Unwinding single molecule BLM RPA chicken optical tweezers structural biology helicase molecular biophysics DNA unwinding
ISSN:	2050-084X, 2050-084X
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Abstract	BLM is a multifunctional helicase that plays critical roles in maintaining genome stability. It processes distinct DNA substrates, but not nicked DNA, during many steps in DNA replication and repair. However, how BLM prepares itself for diverse functions remains elusive. Here, using a combined single-molecule approach, we find that a high abundance of BLMs can indeed unidirectionally unwind dsDNA from a nick when an external destabilizing force is applied. Strikingly, human replication protein A (hRPA) not only ensures that limited quantities of BLMs processively unwind nicked dsDNA under a reduced force but also permits the translocation of BLMs on both intact and nicked ssDNAs, resulting in a bidirectional unwinding mode. This activation necessitates BLM targeting on the nick and the presence of free hRPAs in solution whereas direct interactions between them are dispensable. Our findings present novel DNA unwinding activities of BLM that potentially facilitate its function switching in DNA repair.
AbstractList	BLM is a multifunctional helicase that plays critical roles in maintaining genome stability. It processes distinct DNA substrates, but not nicked DNA, during many steps in DNA replication and repair. However, how BLM prepares itself for diverse functions remains elusive. Here, using a combined single-molecule approach, we find that a high abundance of BLMs can indeed unidirectionally unwind dsDNA from a nick when an external destabilizing force is applied. Strikingly, human replication protein A (hRPA) not only ensures that limited quantities of BLMs processively unwind nicked dsDNA under a reduced force but also permits the translocation of BLMs on both intact and nicked ssDNAs, resulting in a bidirectional unwinding mode. This activation necessitates BLM targeting on the nick and the presence of free hRPAs in solution whereas direct interactions between them are dispensable. Our findings present novel DNA unwinding activities of BLM that potentially facilitate its function switching in DNA repair. BLM is a multifunctional helicase that plays critical roles in maintaining genome stability. It processes distinct DNA substrates, but not nicked DNA, during many steps in DNA replication and repair. However, how BLM prepares itself for diverse functions remains elusive. Here, using a combined single-molecule approach, we find that a high abundance of BLMs can indeed unidirectionally unwind dsDNA from a nick when an external destabilizing force is applied. Strikingly, human replication protein A (hRPA) not only ensures that limited quantities of BLMs processively unwind nicked dsDNA under a reduced force but also permits the translocation of BLMs on both intact and nicked ssDNAs, resulting in a bidirectional unwinding mode. This activation necessitates BLM targeting on the nick and the presence of free hRPAs in solution whereas direct interactions between them are dispensable. Our findings present novel DNA unwinding activities of BLM that potentially facilitate its function switching in DNA repair.BLM is a multifunctional helicase that plays critical roles in maintaining genome stability. It processes distinct DNA substrates, but not nicked DNA, during many steps in DNA replication and repair. However, how BLM prepares itself for diverse functions remains elusive. Here, using a combined single-molecule approach, we find that a high abundance of BLMs can indeed unidirectionally unwind dsDNA from a nick when an external destabilizing force is applied. Strikingly, human replication protein A (hRPA) not only ensures that limited quantities of BLMs processively unwind nicked dsDNA under a reduced force but also permits the translocation of BLMs on both intact and nicked ssDNAs, resulting in a bidirectional unwinding mode. This activation necessitates BLM targeting on the nick and the presence of free hRPAs in solution whereas direct interactions between them are dispensable. Our findings present novel DNA unwinding activities of BLM that potentially facilitate its function switching in DNA repair.
Audience	Academic
Author	Lu, Ying Li, Ming Zhang, Siqi Sun, Bo Xi, Xu-Guang Bi, Lulu Qin, Zhenheng Hou, Xi-Miao Zhang, Xia Modesti, Mauro
Author_xml	– sequence: 1 givenname: Zhenheng surname: Qin fullname: Qin, Zhenheng organization: School of Life Science and Technology, ShanghaiTech University, Shanghai, China, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China, University of Chinese Academy of Sciences, Beijing, China – sequence: 2 givenname: Lulu surname: Bi fullname: Bi, Lulu organization: School of Life Science and Technology, ShanghaiTech University, Shanghai, China – sequence: 3 givenname: Xi-Miao surname: Hou fullname: Hou, Xi-Miao organization: College of Life Sciences, Northwest A&F University, Yangling, China – sequence: 4 givenname: Siqi surname: Zhang fullname: Zhang, Siqi organization: School of Life Science and Technology, ShanghaiTech University, Shanghai, China, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China, University of Chinese Academy of Sciences, Beijing, China – sequence: 5 givenname: Xia surname: Zhang fullname: Zhang, Xia organization: School of Life Science and Technology, ShanghaiTech University, Shanghai, China – sequence: 6 givenname: Ying surname: Lu fullname: Lu, Ying organization: Institute of Physics, Chinese Academy of Sciences, Beijing, China – sequence: 7 givenname: Ming surname: Li fullname: Li, Ming organization: University of Chinese Academy of Sciences, Beijing, China, Institute of Physics, Chinese Academy of Sciences, Beijing, China – sequence: 8 givenname: Mauro orcidid: 0000-0002-4964-331X surname: Modesti fullname: Modesti, Mauro organization: Cancer Research Center of Marseille, CNRS UMR7258, Inserm U1068, Institut Paoli-Calmettes, Aix-Marseille Université, Marseille, France – sequence: 9 givenname: Xu-Guang surname: Xi fullname: Xi, Xu-Guang organization: The LBPA, Ecole Normale Supérieure Paris-Saclay, CNRS, Université Paris Saclay, Gif-sur-Yvette, France – sequence: 10 givenname: Bo orcidid: 0000-0002-4590-7795 surname: Sun fullname: Sun, Bo organization: School of Life Science and Technology, ShanghaiTech University, Shanghai, China
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Keywords	single molecule BLM RPA chicken optical tweezers structural biology helicase molecular biophysics DNA unwinding
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SubjectTerms	BLM Cellular Biology Deoxyribonucleic acid DNA DNA biosynthesis DNA Breaks, Single-Stranded DNA damage DNA helicase DNA repair DNA replication DNA Topoisomerases, Type I - metabolism DNA unwinding DNA, Single-Stranded - metabolism Genomes Genomics helicase Life Sciences Microscopy Novels optical tweezers Proteins RecQ Helicases - metabolism Replication protein A Replication Protein A - metabolism RPA single molecule Structural Biology and Molecular Biophysics Unwinding
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Title	Human RPA activates BLM’s bidirectional DNA unwinding from a nick
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