| Biography | |
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 Prof. Shan-Ho Chou National Chung Hsing University, Chinese Taipei |
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| Title: Diversity of c-di-GMP-binding proteins and mechanisms | |
| Abstract: The discovery of c-di-GMP second messenger was one of the most important breakthroughs in the microbial world in the past two decades. This molecule is present in most bacteria, regulating a plethora variety of important bacterial activities such as biofilm formation, biogenesis and function of flagella and pili, cell differentiation, and biosynthesis of natural product and secretion of pathogenic factors, through binding to an unprecedented array of effectors. There are usually tens or hundreds of enzymes that make or break c-di-GMP in every bacterial genome. However, only a few c-di-GMP receptors have been characterized to date. To get a better understanding of how c-di-GMP carries out its diverse functions, it is of crucial importance to decipher most or all possible c-di-GMP binding motifs. Several c-di-GMP receptors have been found but most of them usually exhibit narrow phylogenetic distribution1. Recently, MshE, an ATPase associated with the mannose-sensitive hemagglutinin type IV pilus formation in Vibrio cholerae, was shown to bind c-di-GMP well by a DRACALA methodology but no canonical binding motif was found in binding c-di-GMP. We have solved the crystal structure of the MshEN/c-di-GMP complex, which revealed an entirely new c-di-GMP binding mode2. It is fused with many other domains such as ATPase, glycosyltransferase, CheA, CheX, REC, cNMP-binding, HD-GYP, and guanylate cyclase, which have been found to play various important roles in bacterial physiology. MshEN is thus a new generation c-di-GMP binding protein that may serve as a good target for developing novel drugs against bacteria without causing drug resistance. (1) Shan-Ho Chou* & Michael Y. Galperin* (2016) (Review) Diversity of c-di-GMP-binding proteins and mechanisms, J. Bacteriology, 198 (1), 32-46. (2) Yu-Chuan Wang, Ko-Hsin Chin, Zhi-Le Tu, Jin He, Christopher J. Jones, David Zamorano Sanchez, Fitnat H. Yildiz, Michael Galperin, & Shan-Ho Chou* (2016) Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain, Nature Communications, 7:12481. | |
| Biography:
Shan-Ho Chou is currently a chair professor of the Institute of Biochemistry, National Chung Hsing University, Taiwan. He received his bachelor’s degree in chemistry from the National Taiwan Normal University, a master’s degree in biochemistry from the National Taiwan University, and a Ph.D. in chemistry from the University of Washington in Seattle, WA, USA. At the first stage of his research career, he mainly studied unusual nucleic acid structures by using two-dimensional nuclear magnetic resonance (NMR) methodology and found several stable nucleic acid structures different from the Watson-Crick base-paired duplex, which were published in review papers in the journals of Nucleic Acids Research, Journal of Molecular Biology, and Trends in Biochemical Science. He then switched to studying structural genomics of the plant pathogen X. campestris by X-ray crystallography and solved several unique c-di-GMP–protein complex structures. He is now combining X-ray, NMR, small-angle X-ray scattering, and cryo-EM techniques to study multidomain proteins associated with c-di-GMP and c-di-AMP binding. He is an author of more than 130 research papers, reviews, and book chapters.
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