The Crystal Structure of TAL Effector PthXo1 Bound to Its DNA Target

Author:

Mak Amanda Nga-Sze1,Bradley Philip2,Cernadas Raul A.3,Bogdanove Adam J.3,Stoddard Barry L.1

Affiliation:

1. Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, A3-025 Seattle, WA 98019, USA.

2. Division of Public Health Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, M1-B514 Seattle, WA 98109, USA.

3. Department of Plant Pathology and Microbiology, Iowa State University, 351 Bessey Hall, Ames, IA 50011, 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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