Expression and characterization of protein disulfide isomerase family proteins in bread wheat.

ABSTRACT:

Background

The major wheat seed proteins are storage proteins that are synthesized in the rough endoplasmic reticulum (ER) of starchy endosperm cells. Many of these proteins have intra- and intermolecular disulfide bonds. In eukaryotes, the formation of most intramolecular disulfide bonds in the ER is thought to be catalyzed by protein disulfide isomerase (PDI) family proteins. The cDNAs that encode eight groups of bread wheat (Triticum aestivum L.) PDI family proteins have been cloned, and their expression levels in developing wheat grains have been determined. The purpose of the present study was to characterize the enzymatic properties of the wheat PDI family proteins and clarify their expression patterns in wheat caryopses.

Results

PDI family cDNAs, which are categorized

SUBMITTER: Kimura S 

PROVIDER: S-EPMC4355359 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature