期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 414, 期 2, 页码 150-158出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0003-9861(03)00122-X
关键词
ribulose 1,5-bisphosphate carboxylase/oxygenase; posttranslational; methylation; protein folding; ribulose 1,5-bisphosphate; activase; oxidation
The life of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco), from gene to protein to irreplaceable component of photosynthetic CO2 assimilation, has successfully served as a model for a number of essential cellular processes centered on protein chemistry and amino acid modifications. Once translated, the two subunits of Rubisco undergo a myriad of co- and posttranslational modifications accompanied by constant interactions with structurally modifying enzymes. Even after final assembly, the essential role played by Rubisco in photosynthetic CO2 assimilation is dependent on continuous conformation modifications by Rubisco activase. Rubisco is also continuously assaulted by various environmental factors, resulting in its turnover and degradation by processes that appear to be enhanced during plant senescence. (C) 2003 Elsevier Science (USA). All rights reserved.
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