Open AccessCrystallization of the plant hormone receptors PYL9/RCAR1, PYL5/RCAR8 and PYR1/RCAR11 in the presence of (+)‐abscisic acid
Author(s) -
Shibata Nobuyuki,
Kagiyama Megumi,
Nakagawa Masahiro,
Hirano Yoshinori,
Hakoshima Toshio
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110007037
Subject(s) - abscisic acid , receptor , plant hormone , hormone , crystallization , chemistry , medicine , botany , biochemistry , biology , organic chemistry , gene
Abscisic acid (ABA) is a plant hormone that plays key regulatory roles in physiological pathways for the adaptation of vegetative tissues to abiotic stresses such as water stress in addition to events pertaining to plant growth and development. The Arabidopsis ABA receptor proteins PYR/PYLs/RCARs form a START family that contains 14 members which are classified into three subfamilies (I–III). Here, purification, crystallization and X‐ray data collection are reported for a member of each of the subfamilies, PYL9/RCAR1 from subfamily I, PYL5/RCAR8 from subfamily II and PYR1/RCAR11 from subfamily III, in the presence of (+)‐abscisic acid. The three proteins crystallize in space groups P 3 1 21/ P 3 2 21, P 2 and P 1, respectively. X‐ray intensity data were collected to 1.9–2.6 Å resolution.