Single Amino Acid Alteration between Valine and Isoleucine Determines the Distinct Pyrabactin Selectivity by PYL1 and PYL2英文文献.pdfVIP

THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 285, NO. 37, pp. 28953–28958, September 10, 2010 © 2010 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in the U.S.A. Single Amino Acid Alteration between Valine and Isoleucine Determines the Distinct Pyrabactin Selectivity by PYL1 and PYL2* Received for publication, June 30, 2010, and in revised form, July 8, 2010 Published, JBC Papers in Press, July 14, 2010, DOI 10.1074/jbc.M110.160192 1 1 1 2 Xiaoqiu Yuan , Ping Yin , Qi Hao , Chuangye Yan, Jiawei Wang, and Nieng Yan From the State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Medicine and School of Life Sciences, Tsinghua University, Beijing 100084, China Abscisic acid (ABA) is one of the most important phytohor- expression of ABA-responsive genes. Structural and biochem- mones in plant. PYL proteins were identified to be ABA recep- ical studies further revealed the molecular basis of ABA-PYL- tors in Arabidopsis thaliana . Despite the remarkably high mediated inhibition of PP2Cs (4–8). Structures of apo- or degree of sequence similarity, PYL1 and PYL2 exhibit distinct ligand-bound PYR1, PYL1, and PYL2 were determined (4–8, responses toward pyrabactin, an ABA agonist. PYL1 inhibits 10). In all of these structures, PYLs are homodimers, with protein phosphatase type 2C upon binding of pyrabactin. In each protomer comprising a conserved ligand-accommodat- contrast, PYL2 appears relatively insensitive to this compound. ing pocket surrounded by four conserved loops CL1–CL4 (4). The