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Brittle-1, an Adenylate Translocator, Facilitates Transfer of Extraplastidial Synthesized ADP-Glucose into Amyloplasts of Maize Endosperms1

Jack C. Shannon*, Fang-Mei Pien, Heping Cao2, and Kang-Chien Liu

Department of Horticulture, 102 Tyson Building, The Pennsylvania State University, University Park, Pennsylvania 16802

Amyloplasts of starchy tissues such as those of maize (Zea mays L.) function in the synthesis and accumulation of starch during kernel development. ADP-glucose pyrophosphorylase (AGPase) is known to be located in chloroplasts, and for many years it was generally accepted that AGPase was also localized in amyloplasts of starchy tissues. Recent aqueous fractionation of young maize endosperm led to the conclusion that 95% of the cellular AGPase was extraplastidial, but immunolocalization studies at the electron- and light-microscopic levels supported the conclusion that maize endosperm AGPase was localized in the amyloplasts. We report the results of two nonaqueous procedures that provide evidence that in maize endosperms in the linear phase of starch accumulation, 90% or more of the cellular AGPase is extraplastidial. We also provide evidence that the brittle-1 protein (BT1), an adenylate translocator with a KTGGL motif common to the ADP-glucose-binding site of starch synthases and bacterial glycogen synthases, functions in the transfer of ADP-glucose into the amyloplast stroma. The importance of the BT1 translocator in starch accumulation in maize endosperms is demonstrated by the severely reduced starch content in bt1 mutant kernels.

1   This work was supported by U.S. Department of Agriculture Competitive Grant no. 94-37306-0737.
2   Present address: Department of Biochemistry and Biophysics, 2154 Molecular Biology Building, Iowa State University, Ames, IA 50011.
*   Corresponding author; e-mail jshannon{at}psu.edu; fax 1-814-863-6139.

Plant Physiol. (1998) 117: 1235-1252
Copyright Clearance Center:   0032-0889/98/117//18
© 1998 American Society of Plant Physiologists




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