Mk. Morell et al., DIFFERENTIAL EXPRESSION AND PROPERTIES OF STARCH BRANCHING ENZYME ISOFORMS IN DEVELOPING WHEAT ENDOSPERM, Plant physiology, 113(1), 1997, pp. 201-208
Three forms of starch branching enzyme (BE) from developing hexaploid
wheat( Triticum aestivum) endosperm have been partially purified and c
haracterized. Immunological cross-reactivities indicate that two forms
(WBE-I-AD, 88 kD, and WBE-I-B, 87 kD) are related to the maize BE I c
lass and that WBE-II (88 kD) is related to maize BE II. Comparison of
the N-terminal sequences from WBE-I-AD and WEE-II with maize and rice
BEs confirms these relationships. Evidence is presented from the analy
sis of nullisomic-tetrasomic wheat lines demonstrating that WEE-I-B is
located on chromosome 7B and that the WBE-I-AD fraction contains poly
peptides that are encoded on chromosomes 7A and 7D. The wheat endosper
m BE classes are differentially expressed during endosperm development
. WBE-II is expressed at a constant level throughout mid and late endo
sperm development. In contrast, WBE-I-AD and WBE-I-B are preferentiall
y expressed in late endosperm development. Differences are also observ
ed in the kinetic characteristics of the enzymes. The WBE-I isoforms h
ave a 2- to 5-fold higher affinity for amylose than does WBE-II, and t
he WEE-I isoforms are activated up to 5-fold by phosphorylated interme
diates and inorganic phosphate, whereas WBE-II is activated only 50%.
The potential implications of this activation of BE I for starch biosy
nthesis are discussed.