Structural Basis for Sequence-Specific Recognition of DNA by TAL Effectors

Author:

Deng Dong12,Yan Chuangye2,Pan Xiaojing12,Mahfouz Magdy3,Wang Jiawei1,Zhu Jian-Kang4,Shi Yigong2,Yan Nieng12

Affiliation:

1. State Key Laboratory of Bio-Membrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China.

2. Tsinghua-Peking Center for Life Sciences, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China.

3. Center for Plant Stress Genomics and Technology, King Abdullah University of Science and Technology, Thuwal 23955-6900, Kingdom of Saudi Arabia.

4. Department of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN 47907, USA.

Abstract

Wrapped DNA TAL effectors are proteins that bacterial pathogens inject into plant cells that bind to host DNA to activate expression of plant genes. The DNA-binding domain of TAL proteins is composed of tandem repeats within which a repeat-variable diresidue sequence confers nucleotide specificity. Deng et al. (p. 720 , published online 5 January) report the structure of the TAL effector dHax3, containing 11.5 repeats, in DNA-free and DNA-bound states, and Mak et al. (p. 716 , published online 5 January) report the structure of the PthXo1 TAL effector, containing 22 repeats, bound to its DNA target. Together, the structures reveal the conformational changes involved in DNA binding and provide the structural basis of DNA recognition.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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