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Biochemical and molecular characterization of a novel starch synthase from potato tubers
Author(s) -
Edwards Anne,
Marshall Jacqueline,
Sidebottom Christopher,
Visser Richard G.F.,
Smith Alison M.,
Martin Cathie
Publication year - 1995
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1995.08020283.x
Subject(s) - starch synthase , atp synthase , starch , chemistry , biochemistry , characterization (materials science) , enzyme , materials science , nanotechnology , amylopectin , amylose
An isoform of starch synthase from potato tubers which is present both in the stroma of the plastid and tightly bound to starch granules has been identified biochemically and a cDNA has been isolated. The protein encoded by the cDNA is 79.9 kDa and has a putative transit peptide and a distinct N‐terminal domain which is predicted to be highly flexible. It is similar in both amino acid sequence and predicted structure to the granule‐bound starch synthase II (GBSSII) of pea embryos. When expressed in Escherichia coli , the mature protein has starch synthase activity. The importance of the isoform has been assessed by biochemical measurements and antisense transformation experiments in which the amount of the isoform in the tuber is severely and specifically reduced. Both approaches indicate that the isoform contributes a maximum of 15% of the total starch synthase activity of the tuber. It is suggested that this isoform and the GBSSII of pea embryos represent a widely distributed class of isoforms of starch synthase. The contribution to total starch synthase activity of members of this class probably varies considerably from one type of storage organ to another.