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Title: Consequences of altering rubisco regulation

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.
Authors:
 [1]
  1. US Dept. of Agriculture (USDA)., Ames, IA (United States)
Publication Date:
OSTI Identifier:
1164812
Report Number(s):
DOE-USDA--ER20268
X08-5347-727; 5347-21000-009-03R; 0414396
DOE Contract Number:
AI02-97ER20268
Resource Type:
Technical Report
Research Org:
US Dept. of Agriculture (USDA)., Ames, IA (United States)
Sponsoring Org:
USDOE
Contributing Orgs:
USDA/ARS/ALARC
Country of Publication:
United States
Language:
English
Subject:
99 GENERAL AND MISCELLANEOUS Photosynthesis; Activase; Rubisco; Arabidopsis