Microbial starch-binding domains are superior to granule-bound starch synthase I for anchoring luciferase to potato starch granules

作     者：Jean-Paul VINCKEN Luc C.J.M. SUURS Richard G.F. VISSER 

作者机构：Laboratory of Plant Breeding Department of Plant Sciences Wageningen University Wageningen The Netherlands 

出 版 物：《Progress in Natural Science:Materials International》 (自然科学进展·国际材料(英文))

年 卷 期：2006年第16卷第12期

页      面：1295-1299页

核心收录：

学科分类：0710[理学-生物学] 071001[理学-植物学] 07[理学] 0805[工学-材料科学与工程（可授工学、理学学位）] 0702[理学-物理学] 

基　　金：Supported by National Natural Science Foundation of China (No .30571183) Jiangsu Education Department (No .JHB04-043) 

主　　题：luciferase GBSS I SBD amf potato. 

摘      要：Microbial starch-binding domains (SBD) and granule-bound starch synthase I (GBSSI) are proteins which are accumulated in potato starch granules. The efficiency of SBD and GBSSI for targeting active luciferase reporter proteins to granules during starch biosynthesis was compared. GBSSI or SBD sequences were fused to the N- or C-terminus of the luciferase (LUC) gene, via an artificial Pro-Thr encoding linker sequence. The genes were introduced into an amylose-free (amf) potato mutant. It appeared that SBD was superior to GBSSI as a targeting sequence, mainly because the luciferase retained higher activity in the SBD-containing fusion proteins than in the GBSSI-containing ones.