CONSEQUENCES OF ALTERING RUBISCO REGULATION

[摘要] Research examined the thermal stability and propensity for aggregation of wild type and the C- and N-terminally modified forms of activase to determine if loss of activity under heat stress is dependent on protein aggregation. The results showed that 1) loss of activity at high temperature is independent of aggregation; 2) activase with both C- and N-terminal S-Tags are more susceptible to aggregation than wild type activase, 3) aggregation is highly dependent on the concentration of Mg2+ and 4) the ATP analog, ATPgammaS, protects against both thermal inactivation and aggregation.

[发布日期] 2013-12-31

[学科分类] 社会科学、人文和艺术（综合）

[关键词] Photosynthesis;Activase;Rubisco;Arabidopsis