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

Q94; Microbial starch-binding domains (SBD) and granule-hound 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 se...

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Veröffentlicht in:Progress in natural science 2006-12, Vol.16 (12), p.1295-1299
Hauptverfasser: Qin, Ji, Vincken, Jean-Paul, Suurs, Luc, Visser, Richard
Format: Artikel
Sprache:eng
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Zusammenfassung:Q94; Microbial starch-binding domains (SBD) and granule-hound 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 (am f) 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.
ISSN:1002-0071
DOI:10.1080/10020070612330144