Site-directed mutagenesis of the ATP-binding site in spinach rubisco activase

Spinach rubisco activase has two isoforms derived from alternate splicing with the larger polypeptide containing an additional 4 kD C-terminal domain. Both isoforms, with molecular masses of 41 kD and 45 kD, were synthesized and purified from the transformed E. coli containing the cDNAs. A significant difference in the kinetics of the ATP response between the two cloned isoforms was observed. The 45 kD polypeptide exhibited sigmoidal kinetics for both rubisco activase and ATPase activities, while the activities of the 41 kD isoform appeared to follow standard Michaelis-Menten kinetics. These observations indicate that the extra C-domain in the 45 kD isoform may play an essential role in controlling the enzyme activity and/or substrate (ATP) binding.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Shen, Jennie Bih-Jien

Contributors dc:contributor

• Ogren, William L.

• Biology, Plant Physiology

Statement dc:rights

• Copyright 1989 Shen, Jennie Bih-Jien

Language dc:language

eng

Identifier

AAI9011016
(UMI)AAI9011016

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/19253