Journal Article

Molecular Cloning, Expression and Subcellular Localization of a BiP Homolog from Rice Endosperm Tissue

Douglas G. Muench, Yujia Wu, Yunsun Zhang, Xingxiang Li, Rebecca S. Boston and Thomas W. Okita

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 38, issue 4, pages 404-412
Published in print January 1997 | ISSN: 0032-0781
Published online January 1997 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a029183
Molecular Cloning, Expression and Subcellular Localization of a BiP Homolog from Rice Endosperm Tissue

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  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry

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The ER luminal binding protein, BiP, has been linked to prolamine protein body formation in rice. To obtain further information on the possible role of this chaperone in protein body formation we have cloned and sequenced a BiP cDNA homolog from rice endosperm. The rice sequence is very similar to the maize BiP exhibiting 92% nu-cleotide identity and 96% deduced amino acid sequence identity in the coding region. Substantial amino acid sequence homology exists between rice BiP and BiP homo-logs from several other plant and animal species including long stretches of conservation through the amino-terminal ATPase domain. Considerable variation, however, is observed within the putative carboxy-terminal peptide-bind-ing domain between the plant and nonplant BiP sequences. A single band of approximately 2.4 kb was visible when RNA gel blots of total RNA purified from seed tissue were probed with radiolabeled rice BiP cDNA. This band increased in intensity during seed development up to 10 days after flowering, and then decreased gradually until seed maturity. Protein gel blots indicated that BiP polypeptide accumulation parallels that of the prolamine polypeptides throughout seed development. Immunocytochemical analysis demonstrated that BiP is localized in a non-stochastic fashion in the endoplasmic reticulum membrane complex of developing endosperm cells. It is abundant on the periphery of the protein inclusion body but not in the central portion of the protein body or in the cisternal ER membranes connecting the protein bodies. These data support a model which proposes that BiP associates with the newly synthesized prolamine polypeptide to facilitate its folding and assembly into a protein inclusion body, and is then recycled.

Keywords: BiP-Endosperm; Prolamine; Protein Body; Rice

Journal Article.  0 words. 

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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