| Literature DB >> 19380351 |
Takayuki Sawada1, Perigio B Francisco, Satomi Aihara, Yoshinori Utsumi, Mayumi Yoshida, Yasunori Oyama, Mikio Tsuzuki, Hikaru Satoh, Yasunori Nakamura.
Abstract
In monocots, starch branching enzyme II (BEII) was functionally differentiated into BEIIa and BEIIb after separation from the dicots, and in cereals BEIIb plays a distinct role in amylopectin biosynthesis in the endosperm. The present study was conducted to examine to what extent a green algal BEII has an overlapping function with BEIIb in starch biosynthesis by introducing the Chlorella BEII gene into an amylose-extender (ae) mutant of rice. Chlorella BEII was found to complement the contribution of the rice endosperm BEIIb to the structures of amylopectin and starch granules because these mutated phenotypes were recovered almost completely to those of the wild type by the expression of Chlorella BEII. When the recombinant BE enzymes were incubated with the rice ae amylopectin, the branching pattern of Chlorella BEII was much more similar to that of rice BEIIb rather than rice BEIIa. Detailed analyses of BE reaction products suggests that BEIIb and Chlorella BEII only transfer chains with a degree of polymerization (DP) of 6 and 7, whereas BEIIa preferably transfers short chains with a DP of about 6-11. These results show that the Chlorella BEII is functionally similar to rice BEIIb rather than BEIIa.Entities:
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Year: 2009 PMID: 19380351 DOI: 10.1093/pcp/pcp058
Source DB: PubMed Journal: Plant Cell Physiol ISSN: 0032-0781 Impact factor: 4.927