SUCROSE SYNTHASE: ELUCIDATION OF COMPLEX POST-TRANSLATIONAL REGULATORY MECHANISMS

Steven C. Huber

关键词: ACTIN;    AVAILABILITY;    DIMERS;    ENZYMES;    IN VITRO;    MAIZE;    METABOLISM;    PLASMA;    PROTEINS;    SACCHAROSE;    SEEDS;    TUBERS Sucrose synthase;    protein phosphorylation;    sugar sensing;    membrane binding;    carbon allocation.;   

DOI  :  10.2172/952234
RP-ID  :  DOE/ER/20031-3
PID  :  OSTI ID: 952234
Others  :  TRN: US201120%%328

学科分类：生物科学（综合）

美国|英语

来源: SciTech Connect

【 摘 要 】

Studies have focused on the enzyme sucrose synthase, which plays an important role in the metabolism of sucrose in seeds and tubers. There are three isoforms of SUS in maize, referred to as SUS1, SUS-SH1, and SUS2. SUS is generally considered to be tetrameric protein but recent evidence suggests that SUS can also occur as a dimeric protein. The formation of tetrameric SUS is regulated by sucrose concentration in vitro and this could also be an important factor in the cellular localization of the protein. We found that high sucrose concentrations, which promote tetramer formation, also inhibit the binding of SUS1 to actin filaments in vitro. Previously, high sucrose concentrations were shown to promote SUS association with the plasma membrane. The specific regions of the SUS molecule involved in oligomerization are not known, but we identified a region of the SUS1 moelcule by bioinformatic analysis that was predicted to form a coiled coil. We demonstrated that this sequence could, in fact, self-associate as predicted for a coiled coil, but truncation analysis with the full-length recombinant protein suggested that it was not responsible for formation of dimers or tetramers. However, the coiled coil may function in binding of other proteins to SUS1. Overall, sugar availability may differentially influence the binding of SUS to cellular structures, and these effects may be mediated by changes in the oligomeric nature of the enzyme.