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Plant Physiol, March 2001, Vol. 125, pp. 1406-1418
Molecular Structure of Three Mutations at the Maize
sugary1 Locus and Their Allele-Specific
Phenotypic Effects1
Jason R.
Dinges,
Christophe
Colleoni,
Alan M.
Myers, and
Martha G.
James*
Department of Biochemistry, Biophysics, and Molecular Biology, Iowa
State University, Ames, Iowa 50011
Starch production in all plants examined is altered by mutations of
isoamylase-type starch-debranching enzymes (DBE), although how these
proteins affect glucan polymer assembly is not understood. Various
allelic mutations in the maize (Zea mays) gene
sugary1 (su1), which codes for an
isoamylase-type DBE, condition distinct kernel phenotypes. This study
characterized the recessive mutations su1-Ref,
su1-R4582::Mu1, and su1-st,
regarding their molecular basis, chemical phenotypes, and effects on
starch metabolizing enzymes. The su1-Ref allele results
in two specific amino acid substitutions without affecting the Su1 mRNA
level. The su1-R4582::Mu1 mutation is a null
allele that abolishes transcript accumulation. The
su1-st mutation results from insertion of a novel
transposon-like sequence, designated Toad, which causes
alternative pre-mRNA splicing. Three su1-st mutant
transcripts are produced, one that is nonfunctional and two that code
for modified SU1 polypeptides. The su1-st mutation is
dominant to the null allele su1-R4582::Mu1,
but recessive to su1-Ref, suggestive of complex effects
involving quaternary structure of the SU1 enzyme. All three
su1- alleles severely reduce or eliminate isoamylase-type DBE activity, although su1-st kernels
accumulate less phytoglycogen and Suc than su1-Ref or
su1-R4582::Mu1 mutants. The chain length
distribution of residual amylopectin is significantly altered by
su1-Ref and su1-R4582::Mu1,
whereas su1-st has modest effects. These results,
together with su1 allele-specific effects on other
starch- metabolizing enzymes detected in zymograms, suggest that total
DBE catalytic activity is the not the sole determinant of
Su1 function and that specific interactions between SU1
and other components of the starch biosynthetic system are required.
1
This work was supported by the U.S. Department
of Agriculture (grant no. 99-35304-8642 to M.G.J. and A.M.M.), by a
U.S. Department of Agriculture National Needs Fellowship in Plant
Biotechnology (grant no. 98-38420-5838 to J.R.D.), and by the
National Science Foundation (grant no. DIR-9113593 to the Iowa State
University Signal Transduction Training Group). This is a journal paper
(no. J-19209) of the Iowa Agriculture and Home Economics Experiment Station (Ames; project no. 3593).
*
Corresponding author; e-mail mgjames{at}iastate.edu; fax
515-294-0453.
© 2001 American Society of Plant Physiologists
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