TY - JOUR
T1 - A role for the cysteine-rich 10 kDa prolamin in protein body i formation in rice
AU - Nagamine, Ai
AU - Matsusaka, Hiroaki
AU - Ushijima, Tomokazu
AU - Kawagoe, Yasushi
AU - Ogawa, Masahiro
AU - Okita, Thomas W.
AU - Kumamaru, Toshihiro
N1 - Funding Information:
This work was supported by the Japan Society for the Promotion of Science [grant-in-aid for Scientific Research to T.K. (16380009 and 21380008]; Bio-oriented Technology Research Advanced Institution (BRAIN) [the program for Promotion of Basic Research Activities for Innovative Biosciences]; the Ministry of Agriculture, Forestry and Fisheries of Japan [grant to Y.K. (Genomics for Agricultural Innovation, IPG-0023); United States National Science Foundation [grants IOS-1021699 and DBI-0605016 to T.W.O.]. United States Department of Agriculture-Cooperative State Research, Education and Extension-National Research Initiative [grant 2006-35301-17043 to T.W.O.].
PY - 2011/6
Y1 - 2011/6
N2 - The rice prolamins consist of cysteine-rich 10 kDa (CysR10), 14 kDa (CysR14) and 16 kDa (CysR16) molecular species and a cysteine-poor 13 kDa (CysP13) polypeptide. These storage proteins form protein bodies (PBs) composed of single spherical intracisternal inclusions assembled within the lumen of the rough endoplasmic reticulum. Immunofluorescence and immunoelectron microscopy demonstrated that CysR10 and CysP13 were asymmetrically distributed within the PBs, with the former concentrated at the electron-dense center core region and the latter distributed mainly to the electron-lucent peripheral region. These results together with temporal expression data showed that the formation of prolamin-containing PB-I in the wild-type endosperm was initiated by the accumulation of CysR10 to form the center core. In mutants deficient for cysteine-rich prolamins, the typical PB-I structures containing the electron-dense center core were not observed, and instead were replaced by irregularly shaped, electron-lucent, hypertrophied PBs. Similar, deformed PBs were observed in a CysR10 RNA interference plant line. These results suggest that CysR10, through its formation of the central core and its possible interaction with other cysteine-rich prolamins, is required for tight packaging of the proteins into a compact spherical structure.
AB - The rice prolamins consist of cysteine-rich 10 kDa (CysR10), 14 kDa (CysR14) and 16 kDa (CysR16) molecular species and a cysteine-poor 13 kDa (CysP13) polypeptide. These storage proteins form protein bodies (PBs) composed of single spherical intracisternal inclusions assembled within the lumen of the rough endoplasmic reticulum. Immunofluorescence and immunoelectron microscopy demonstrated that CysR10 and CysP13 were asymmetrically distributed within the PBs, with the former concentrated at the electron-dense center core region and the latter distributed mainly to the electron-lucent peripheral region. These results together with temporal expression data showed that the formation of prolamin-containing PB-I in the wild-type endosperm was initiated by the accumulation of CysR10 to form the center core. In mutants deficient for cysteine-rich prolamins, the typical PB-I structures containing the electron-dense center core were not observed, and instead were replaced by irregularly shaped, electron-lucent, hypertrophied PBs. Similar, deformed PBs were observed in a CysR10 RNA interference plant line. These results suggest that CysR10, through its formation of the central core and its possible interaction with other cysteine-rich prolamins, is required for tight packaging of the proteins into a compact spherical structure.
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U2 - 10.1093/pcp/pcr053
DO - 10.1093/pcp/pcr053
M3 - Article
C2 - 21521743
AN - SCOPUS:79958782248
SN - 0032-0781
VL - 52
SP - 1003
EP - 1016
JO - Plant and Cell Physiology
JF - Plant and Cell Physiology
IS - 6
ER -