Structural basis for sequence-specific recognition of DNA by TAL effectors

Handle URI:
http://hdl.handle.net/10754/562055
Title:
Structural basis for sequence-specific recognition of DNA by TAL effectors
Authors:
Deng, Dong; Yan, Chuangye; Pan, Xiaojing; Mahfouz, Magdy M. ( 0000-0002-0616-6365 ) ; Wang, Jiawei; Zhu, Jiankang; Shi, Yi Gong; Yan, Nieng
Abstract:
TAL (transcription activator-like) effectors, secreted by phytopathogenic bacteria, recognize host DNA sequences through a central domain of tandem repeats. Each repeat comprises 33 to 35 conserved amino acids and targets a specific base pair by using two hypervariable residues [known as repeat variable diresidues (RVDs)] at positions 12 and 13. Here, we report the crystal structures of an 11.5-repeat TAL effector in both DNA-free and DNA-bound states. Each TAL repeat comprises two helices connected by a short RVD-containing loop. The 11.5 repeats form a right-handed, superhelical structure that tracks along the sense strand of DNA duplex, with RVDs contacting the major groove. The 12th residue stabilizes the RVD loop, whereas the 13th residue makes a base-specific contact. Understanding DNA recognition by TAL effectors may facilitate rational design of DNA-binding proteins with biotechnological applications.
KAUST Department:
Center for Desert Agriculture; Bioscience Program; Biological and Environmental Sciences and Engineering (BESE) Division
Publisher:
American Association for the Advancement of Science (AAAS)
Journal:
Science
Issue Date:
5-Jan-2012
DOI:
10.1126/science.1215670
PubMed ID:
22223738
PubMed Central ID:
PMC3586824
Type:
Article
ISSN:
00368075
Sponsors:
We thank J. He and Q. Wang at Shanghai Synchrotron Radiation Facility (SSRF) beamline BL17U and K. Hasegawa and T. Kumasaka at the Spring-8 beamline BL41XU for on-site assistance. This work was supported by funds from the Ministry of Science and Technology (grant numbers 2009CB918801, 2009CB918802, and 2011CB910501); projects 30888001, 91017011, and 31070644 of the National Natural Science Foundation of China; and Tsinghua University 985 Phase II funds. Coordinates and structure factors for the DNA-free and DNA-bound structures have been deposited with the Protein Data Bank under accession codes 3V6P and 3V6T.
Additional Links:
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3586824
Appears in Collections:
Articles; Bioscience Program; Center for Desert Agriculture; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorDeng, Dongen
dc.contributor.authorYan, Chuangyeen
dc.contributor.authorPan, Xiaojingen
dc.contributor.authorMahfouz, Magdy M.en
dc.contributor.authorWang, Jiaweien
dc.contributor.authorZhu, Jiankangen
dc.contributor.authorShi, Yi Gongen
dc.contributor.authorYan, Niengen
dc.date.accessioned2015-08-03T09:43:42Zen
dc.date.available2015-08-03T09:43:42Zen
dc.date.issued2012-01-05en
dc.identifier.issn00368075en
dc.identifier.pmid22223738en
dc.identifier.doi10.1126/science.1215670en
dc.identifier.urihttp://hdl.handle.net/10754/562055en
dc.description.abstractTAL (transcription activator-like) effectors, secreted by phytopathogenic bacteria, recognize host DNA sequences through a central domain of tandem repeats. Each repeat comprises 33 to 35 conserved amino acids and targets a specific base pair by using two hypervariable residues [known as repeat variable diresidues (RVDs)] at positions 12 and 13. Here, we report the crystal structures of an 11.5-repeat TAL effector in both DNA-free and DNA-bound states. Each TAL repeat comprises two helices connected by a short RVD-containing loop. The 11.5 repeats form a right-handed, superhelical structure that tracks along the sense strand of DNA duplex, with RVDs contacting the major groove. The 12th residue stabilizes the RVD loop, whereas the 13th residue makes a base-specific contact. Understanding DNA recognition by TAL effectors may facilitate rational design of DNA-binding proteins with biotechnological applications.en
dc.description.sponsorshipWe thank J. He and Q. Wang at Shanghai Synchrotron Radiation Facility (SSRF) beamline BL17U and K. Hasegawa and T. Kumasaka at the Spring-8 beamline BL41XU for on-site assistance. This work was supported by funds from the Ministry of Science and Technology (grant numbers 2009CB918801, 2009CB918802, and 2011CB910501); projects 30888001, 91017011, and 31070644 of the National Natural Science Foundation of China; and Tsinghua University 985 Phase II funds. Coordinates and structure factors for the DNA-free and DNA-bound structures have been deposited with the Protein Data Bank under accession codes 3V6P and 3V6T.en
dc.publisherAmerican Association for the Advancement of Science (AAAS)en
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3586824en
dc.titleStructural basis for sequence-specific recognition of DNA by TAL effectorsen
dc.typeArticleen
dc.contributor.departmentCenter for Desert Agricultureen
dc.contributor.departmentBioscience Programen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalScienceen
dc.identifier.pmcidPMC3586824en
dc.contributor.institutionState Key Laboratory of Bio-Membrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, Chinaen
dc.contributor.institutionTsinghua-Peking Center for Life Sciences, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, Chinaen
dc.contributor.institutionDepartment of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN 47907, United Statesen
kaust.authorMahfouz, Magdy M.en

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