Structural basis of the TAL effector–DNA interaction
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Matthias Bochtler
Matthias Bochtler completed a PhD with Prof. Robert Huber at TU Munich and the Max-Planck-Institute of Biochemistry on bacterial model systems of the proteasome. He has since been a group leader at the Max-Planck-Institute of Molecular and Cell Biology running an outstation at the International Institute of Molecular and Cell Biology (IIMCB) in Warsaw, Poland, and at Cardiff University in Wales, UK. In 2011, he returned as a group leader to the IIMCB and now also holds a professorship at the neighboring Institute of Biochemistry and Biophysics (IBB) of the Polish Academy of Sciences. His current research interests center on the structural biology of protein nucleic acid interactions and on DNA methylation.
Abstract
Phytopathogen transcription activator-like effectors (TALEs) bind DNA in a sequence specific manner in order to manipulate host transcription. TALE specificity correlates with repeat variable diresidues in otherwise highly stereotypical 34–35mer repeats. Recently, the crystal structures of two TALE DNA-binding domains have illustrated the molecular basis of the TALE cipher. The structures show that the TALE repeats form a right-handed superhelix that is wound around largely undistorted B-DNA to match its helical parameters. Surprisingly, repeat variable residue 1 is not in contact with the bases. Instead, it is involved in hydrogen bonding interactions that stabilize the overall structure of the protein. Repeat variable residue 2 contacts the top strand base and forms sequence-specific hydrogen bonds and/or van der Waals contacts. Very unexpectedly, bottom strand bases are exposed to solvent and do not make any direct contacts with the protein. This review contains a summary of TALE biology and applications and a detailed description of the recent breakthroughs that have provided insights into the molecular basis of the TALE code.
About the author
Matthias Bochtler completed a PhD with Prof. Robert Huber at TU Munich and the Max-Planck-Institute of Biochemistry on bacterial model systems of the proteasome. He has since been a group leader at the Max-Planck-Institute of Molecular and Cell Biology running an outstation at the International Institute of Molecular and Cell Biology (IIMCB) in Warsaw, Poland, and at Cardiff University in Wales, UK. In 2011, he returned as a group leader to the IIMCB and now also holds a professorship at the neighboring Institute of Biochemistry and Biophysics (IBB) of the Polish Academy of Sciences. His current research interests center on the structural biology of protein nucleic acid interactions and on DNA methylation.
©2012 by Walter de Gruyter Berlin Boston
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Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- No end in sight: the development of protein crystallography in Martinsried
- Highlight: No End in Sight: The Development of Protein Crystallography in Martinsried
- Functional and structural insights into astacin metallopeptidases
- β-Trefoil inhibitors – from the work of Kunitz onward
- Structural basis of the TAL effector–DNA interaction
- Nature’s way of handling a greenhouse gas: the copper-sulfur cluster of purple nitrous oxide reductase
- Rustless translation
- Structural basis of [NiFe] hydrogenase maturation by Hyp proteins
- Covalent and non-covalent reversible proteasome inhibition
- Structural origins of AGC protein kinase inhibitor selectivities: PKA as a drug discovery tool
- Structural analysis of the C-terminal domain of the spliceosomal helicase Prp22
- N-terminal acetylation of annexin A2 is required for S100A10 binding
- Withaferin A binds covalently to the N-terminal domain of annexin A2
- PhoB transcriptional activator binds hierarchically to pho box promoters
- Research Articles/Short Communications
- Protein Structure and Function
- Biochemical and functional characterization of human phospholipid scramblase 4 (hPLSCR4)
- Cell Biology and Signaling
- Dual-specificity phosphatases are targets of the Wnt/β-catenin pathway and candidate mediators of β-catenin/Ras signaling interactions
- Proteolysis
- Inhibition of Aeromonas sobria serine protease (ASP) by α2-macroglobulin
