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Production and characterization of novel glycogen-based polymer. Joint research by Public University of Navarra and Niigata University

AutorFukushima, Mamiko; Almagro, Goizeder ; Hanashiro, Isao; Pozueta Romero, Javier ; Mitsui, Toshiaki; Itoh, Kimiko
Fecha de publicaciónsep-2015
CitaciónKAAB International Symposium (2015)
ResumenNatural storage polysaccharides, like as amylopectin and glycogen, vary in form and molecular size. Glycogen molecule is smaller in size and higher in branching degree than that of amylopectin. To develop a novel type of glycogen containing a long α-1, 4 glucosyl chain, we introduced rice granule-bound starch synthase I (GBSSI) gene in Escherichia coli and analyzed its expression and effect on glycogen synthesis, Rice GBSSI synthesizes not only amylose but also amylopectin, especially synthesizes extra-long chain, whose degrees of polymerization is over one hundred (1). We constructed the expression vector, pHis:SUMO:GBSSI, and confirmed that the expressed His:SUMO:GBSSI can synthesize extra-long chain in amylopectin in vitro. We transformed the pHis:SUMO:GBSSI into various E. coli strains, BW25113 and its mutants deficient in genes related to glycogen accumulation (Keio Collection)(2,3), and then examined effect of GBSSI expression on changes in nature and the amount of glycogen. Genes involved in Glycogen metabolism in E. coli are clustered in two apparently independent transcriptional units, glgBX (encoding branching enzyme GlgB and debranching enzyme GlgX) and glgCAP (encoding ADPG pyrophosphorylase GlgC, glycogen synthase GlgA and glycogen phosphorylase GlgP),. Both of ΔglgX andΔglgP mutants show increase in glycogen accumulation than BW25113, whileΔglgA mutant accumulates no glycogen at all. We use these three mutants,ΔglgX, ΔglgP, and ΔglgA, for this study. GBSSI expressing ΔglgX,ΔglgP, and BW25113 produced much more glycogen than non-expressing E. coli mutants, whereas the GBSSI expressing mutant ΔglgA did not produce the glycogen at all. The results indicate that the rice GBSSI does not complement the glycogen synthase deficiency by ΔglgA in E. coli. Our research also indicates that GBSSI can function not only in rice, but also in E. coli and affect its glycogen accumulation.
DescripciónTrabajo presentado en el KAAB International Symposium (Frontiers in Plant Science and Biotechnology), celebrado en Niigata (Japón) el 29 de septiembre de 2015.
URIhttp://hdl.handle.net/10261/142378
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