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

Dong Deng; Chuangye Yan; Xiaojing Pan; Magdy M. Mahfouz; Jiawei Wang; Jian-Kang Zhu; Yi Gong Shi; Nieng Yan

doi:10.1126/science.1215670

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

Dong Deng, Chuangye Yan, Xiaojing Pan, Magdy M. Mahfouz, Jiawei Wang, Jian-Kang Zhu, Yi Gong Shi, Nieng Yan

Research output: Contribution to journal › Article › peer-review

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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.

Original language	English (US)
Pages (from-to)	720-723
Number of pages	4
Journal	Science
Volume	335
Issue number	6069
DOIs	https://doi.org/10.1126/science.1215670
State	Published - Jan 6 2012

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: 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.

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10.1126/science.1215670

https://repository.kaust.edu.sa/bitstream/10754/562055/1/Articlefile1.pdf

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title = "Structural basis for sequence-specific recognition of DNA by TAL effectors",

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.",

author = "Dong Deng and Chuangye Yan and Xiaojing Pan and Mahfouz, {Magdy M.} and Jiawei Wang and Jian-Kang Zhu and Shi, {Yi Gong} and Nieng Yan",

note = "KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: 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.",

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T1 - Structural basis for sequence-specific recognition of DNA by TAL effectors

AU - Deng, Dong

AU - Yan, Chuangye

AU - Pan, Xiaojing

AU - Mahfouz, Magdy M.

AU - Wang, Jiawei

AU - Zhu, Jian-Kang

AU - Shi, Yi Gong

AU - Yan, Nieng

N1 - KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: 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.

PY - 2012/1/6

Y1 - 2012/1/6

N2 - 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.

AB - 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.

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JO - Science

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ER -

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

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