Binding-protein expression is subject to temporal, developmental and stress-induced regulation in terminally differentiated soybean organs
- 1 February 1995
- journal article
- research article
- Published by Springer Nature in Planta
- Vol. 195 (4) , 611-621
- https://doi.org/10.1007/bf00195722
Abstract
Binding protein (BiP) is a widely distributed and highly conserved endoplasmic-reticulum luminal protein that has been implicated in cotranslational folding of nascent polypeptides, and in the recognition and disposal of misfolded polypeptides. Analysis of cDNA sequences and genomic blots indicates that soybeans (Glycine max L. Merr.) possess a small gene family encoding BiP. The deduced sequence of BiP is very similar to that of other plant BiPs. We have examined the expression of BiP in several different terminally differentiated soybean organs including leaves, pods and seed cotyledons. Expression of BiP mRNA increases during leaf expansion while levels of BiP protein decrease. Leaf BiP mRNA is subject to temporal control, exhibiting a large difference in expression in a few hours between dusk and night. The expression of BiP mRNA varies in direct correlation with accumulation of seed storage proteins. The hybridization suggests that maturing-seed BiP is likely to be a different isoform from vegetative BiPs. Levels of BiP protein in maturing seeds vary with BiP mRNA. High levels of BiP mRNA are detected after 3 d of seedling growth. Little change in either BiP mRNA or protein levels was detected in maturing soybean pods, although BiP-protein levels decrease in fully mature pods. Persistent wounding of leaves by whiteflies induces massive overexpression of BiP mRNA while only slightly increasing BiP-protein levels. In contrast single-event puncture wounding only slightly induces additional BiP expression above the temporal variations. These observations indicate that BiP is not constitutively expressed in terminally differentiated plant organs. Expression of BiP is highest during the developmental stages of leaves, pods and seeds when their constituent cells are producing seed or vegetative storage proteins, and appears to be subject to complex regulation, including developmental, temporal and wounding. The mention of vendor or product does not imply that they are endorsed or recommended by the U.S. Department of Agriculture over vendors of similar products not mentioned.Keywords
This publication has 51 references indexed in Scilit:
- Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocationCell, 1993
- Long-term sensitization training in Aplysia leads to an increase in the expression of BiP, the major protein chaperon of the ER.The Journal of cell biology, 1992
- Protein sorting to the vacuolar membrane.Plant Cell, 1992
- Bean homologs of the mammalian glucose‐regulated proteins: induction by tunicamycin and interaction with newly synthesized seed storage proteins in the endoplasmic reticulumThe Plant Journal, 1992
- Sec61p and BiP directly facilitate polypeptide translocation into the ERCell, 1992
- Gibberellic Acid Regulates the Level of a BiP Cognate in the Endoplasmic Reticulum of Barley Aleurone CellsPlant Physiology, 1991
- Transcriptional regulation by a circadian rhythm.Plant Cell, 1989
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Influence of Opaque-2 and Floury-2 Genes on Formation of Proteins in Particulates of Corn EndospermPlant Physiology, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970