TY - JOUR
T1 - Storage protein accumulation in developing rice (Oryza sativa L.) seeds
AU - Luthe, Dawn Sywassink
N1 - Funding Information:
This research was supported by the Mississippi Agricultural and Forestry Experiment Station. MAFES Publication No. 5380. I would like to thank Dr. James C. Delouche for planting the rice and tagging it at anthesis. The technical assistance of Mr. Hernan Rossi and Ms. Tracey Colyer is greatly appreciated. I would also like to acknowledge Ms. Nik Abdul Rahman for her preliminary studies on rice storage proteins.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1983
Y1 - 1983
N2 - Rice (Oryza sativa L.) panicles were harvested at 2-day intervals from 4-20 days post anthesis (DPA) and labeled with [35S]sulfate. The amount of protein synthesis at each sampling date was estimated by determining the amount of exogenously applied [35S]sulfate incorporated into acid-precipitable material. The largest amount of incorporation occurred at 8 DPA and decreased after 10 DPA. When total seed extracts were analyzed by sodium dodecyl sulfate-polyacrylamine gel electrophoresis (SDS-PAGE), the 35-39 and 20 kilodalton (kd) groups of polypeptides appeared as early as 6 DPA. When these polypeptides were compared with those of globulin, prolamin and glutelin fractions sequentially extracted from rice flour, they had the same electrophoretic mobility as glutelin. The largest accumulation of polypeptides occurred between 8 and 10 DPA. When radioactive peptides from seeds labeled in vivo were visualized by fluorography, there was a prominent 56-kd polypeptide but no polypeptides co-migrating with glutelin were evident. A pulse-chase experiment indicated that the 56-kd polypeptide could be chased into the 35-39 and 20 kd groups. Translation in vitro suggests that the 56-kd polypeptide was preferentially synthesized by membrane-bound polysomes.
AB - Rice (Oryza sativa L.) panicles were harvested at 2-day intervals from 4-20 days post anthesis (DPA) and labeled with [35S]sulfate. The amount of protein synthesis at each sampling date was estimated by determining the amount of exogenously applied [35S]sulfate incorporated into acid-precipitable material. The largest amount of incorporation occurred at 8 DPA and decreased after 10 DPA. When total seed extracts were analyzed by sodium dodecyl sulfate-polyacrylamine gel electrophoresis (SDS-PAGE), the 35-39 and 20 kilodalton (kd) groups of polypeptides appeared as early as 6 DPA. When these polypeptides were compared with those of globulin, prolamin and glutelin fractions sequentially extracted from rice flour, they had the same electrophoretic mobility as glutelin. The largest accumulation of polypeptides occurred between 8 and 10 DPA. When radioactive peptides from seeds labeled in vivo were visualized by fluorography, there was a prominent 56-kd polypeptide but no polypeptides co-migrating with glutelin were evident. A pulse-chase experiment indicated that the 56-kd polypeptide could be chased into the 35-39 and 20 kd groups. Translation in vitro suggests that the 56-kd polypeptide was preferentially synthesized by membrane-bound polysomes.
UR - http://www.scopus.com/inward/record.url?scp=0038342504&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0038342504&partnerID=8YFLogxK
U2 - 10.1016/0304-4211(83)90110-4
DO - 10.1016/0304-4211(83)90110-4
M3 - Article
AN - SCOPUS:0038342504
SN - 0304-4211
VL - 32
SP - 147
EP - 158
JO - Plant Science Letters
JF - Plant Science Letters
IS - 1-2
ER -