The developing endosperm of rice (Oryza sativa) synthesizes
large amounts of structurally and physicochemically diverse
proteins, which serve as nutritional reserves for germinating seedlings.
Disulfide bonds, which covalently link pairs of Cys residues
and impart thermodynamic stability to proteins [1], permit redox
control of protein packaging into and releasing from storage
organelles. Only natively folded proteins with correct patterns of
disulfide bonds can be transported from the endoplasmic reticulum
(ER) to protein storage organelles [2]. For example, highly
hydrophobic prolamins are packed into ER-derived protein body
(designated PB-I) within the ER by a polymerization process
involving the formation of intermolecular disulfide bonds [3],
and proglutelins, which are composed of acidic and basic subunits,
acquire intramolecular disulfide bonds before being transported
from the ER to protein storage vacuole-derived protein body
(designated PB-II) [4].
The ER contains enzymes that mediate the formation of disulfide
bonds in proteins undergoing the folding process. Protein disulfide
isomerases (PDIs), a family of thiol-disulfide oxidoreductases that
The developing endosperm of rice (Oryza sativa) synthesizes
large amounts of structurally and physicochemically diverse
proteins, which serve as nutritional reserves for germinating seedlings.
Disulfide bonds, which covalently link pairs of Cys residues
and impart thermodynamic stability to proteins [1], permit redox
control of protein packaging into and releasing from storage
organelles. Only natively folded proteins with correct patterns of
disulfide bonds can be transported from the endoplasmic reticulum
(ER) to protein storage organelles [2]. For example, highly
hydrophobic prolamins are packed into ER-derived protein body
(designated PB-I) within the ER by a polymerization process
involving the formation of intermolecular disulfide bonds [3],
and proglutelins, which are composed of acidic and basic subunits,
acquire intramolecular disulfide bonds before being transported
from the ER to protein storage vacuole-derived protein body
(designated PB-II) [4].
The ER contains enzymes that mediate the formation of disulfide
bonds in proteins undergoing the folding process. Protein disulfide
isomerases (PDIs), a family of thiol-disulfide oxidoreductases that
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