The endoplasmic reticulum chaperone binding protein (BiP) is important in
protein synthesis, folding assembly, and secretion. To study the role of BiP
in seed development of wheat, Capital Normal University's Yueming Yan and
Xiaohui Li, and their team, cloned three BiP cDNA sequences in bread wheat
(Triticum aestivum) and examined its expression.

Analysis showed that BiPs contain three highly conserved domains present in
plants, animals, and microorganisms, indicating evolutionary conservation.
It was also found that TaBiP (Triticum aestivum BiP) gene expression was
predominantly localized to seed endosperm. Drought stress also significantly
up-regulated the expression of TaBiPs in roots, leaves, and developing
grains.

The high conservation of BiP sequences suggests that it plays the same role
across species. The expression of TaBiP enzymes in different wheat tissues
and under abiotic stress indicates that it is abundant in tissues with high
secretory activity and with the high number of cells undergoing division.
TaBiP genes are regulated during seed development and early seedling growth,
and under various abiotic stresses.

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