2'-Carboxy-D-arabitinol 1-phosphate protects ribulose 1,5-bisphosphate carboxylase/oxygenase against proteolytic breakdown

A - Papers appearing in refereed journals

Khan, S., Andralojc, P. J., Lea, P. J. and Parry, M. A. J. 1999. 2'-Carboxy-D-arabitinol 1-phosphate protects ribulose 1,5-bisphosphate carboxylase/oxygenase against proteolytic breakdown. European Journal of Biochemistry. 266 (3), pp. 840-847.

AuthorsKhan, S., Andralojc, P. J., Lea, P. J. and Parry, M. A. J.
Abstract

Trypsin-catalysed cleavage of purified ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) and the resultant irreversible loss of carboxylase activity were prevented by prior incubation with the naturally occurring nocturnal Rubisco inhibitor 2'-carboxy-D-arabitinol 1-phosphate (CA1P), as well as with ribulose 1,5-bisphosphate (RuBP, Mg2+ and CO2. CA1P also protected Rubisco from loss of activity caused by carboxypeptidase A. When similar experiments were carried out using soluble chloroplast proteases, CA1P was again able to protect Rubisco against proteolytic degradation and the consequent irreversible loss of catalytic activity. Thus, CA1P prevents the proteolytic breakdown of Rubisco by endogenous and exogenous proteases. In this way, CA1P may affect the amounts of Rubisco protein available for photosynthetic CO2 assimilation. Rubisco turnover tin the presence of RuBP, Mg2+ and CO2) may confer similar protection against proteases in the Light.

KeywordsBiochemistry & Molecular Biology
Year of Publication1999
JournalEuropean Journal of Biochemistry
Journal citation266 (3), pp. 840-847
Digital Object Identifier (DOI)doi:10.1046/j.1432-1327.1999.00913.x
PubMed ID10583377
Open accessPublished as non-open access
Funder project or code214
414
ISSN00142956
PublisherWiley

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