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THE PLANT CELL, Vol 9, Issue 11 2037-2050, Copyright © 1997 by American Society of Plant Biologists
Role of the Sulfhydryl Redox State and Disulfide Bonds in Processing and Assembly of 11S Seed Globulins
R. Jung, Y. W. Nam, I. Saalbach, K. Muntz and N. C. Nielsen
United States Department of Agriculture, Agricultural Research Service, and the Departments of Agronomy and Biochemistry, Purdue University, West Lafayette, Indiana 47907-1150
Seed legumins contain two conserved disulfide bonds: an interchain bond
(IE) connecting the acidic and basic chains and an intrachain bond (IA)
internal to the acidic chain. Mutant subunits were constructed in which
these disulfide bonds were disrupted. Oxidized glutathione stimulated the
rate of assembly of trimers with unmodified prolegumin subunits.
Stimulation was not detected during assembly of IE mutant subunits and was
diminished for the IA mutant. Hexamer assembly with trimers of mature
unmodified subunits required oxidizing conditions. Trimers composed of
mature IE mutants did not form hexamers. Both mutant and non-mutant
subunits accumulated in hexamers when the cDNAs were expressed in tobacco.
Hexamer assembly in seeds probably involved trimers with a mixture of
mutant and non-mutant subunits. Similarly, mixed trimers that were a
mixture of mutant and non-mutant subunits assembled into hexamers in vitro.
The results demonstrate the importance of disulfide bonds during the
assembly of 11S globulins.
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