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Originally published In Press as doi:10.1074/jbc.M004580200 on June 16, 2000

J. Biol. Chem., Vol. 275, Issue 34, 26241-26244, August 25, 2000
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Activase Region on Chloroplast Ribulose-1,5-bisphosphate Carboxylase/Oxygenase
NONCONSERVATIVE SUBSTITUTION IN THE LARGE SUBUNIT ALTERS SPECIES SPECIFICITY OF PROTEIN INTERACTION*

Carolyn M. OttDagger §, Bryan D. SmithDagger , Archie R. Portis Jr.||, and Robert J. SpreitzerDagger **

From the Dagger  Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588 and || Department of Crop Sciences, University of Illinois and Photosynthesis Research Unit, Agricultural Research Service, United States Department of Agriculture, Urbana, Illinois 61801

In the active form of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39), a carbamate at lysine 201 binds Mg2+, which then interacts with the carboxylation transition state. Rubisco activase facilitates this spontaneous carbamylation/metal-binding process by removing phosphorylated inhibitors from the Rubisco active site. Activase from Solanaceae plants (e.g. tobacco) fails to activate Rubisco from non-Solanaceae plants (e.g. spinach and Chlamydomonas reinhardtii), and non-Solanaceae activase fails to activate Solanaceae Rubisco. Directed mutagenesis and chloroplast transformation previously showed that a proline 89 to arginine substitution on the surface of the large subunit of Chlamydomonas Rubisco switched its specificity from non-Solanaceae to Solanaceae activase activation. To define the size and function of this putative activase binding region, substitutions were created at positions flanking residue 89. As in the past, these substitutions changed the identities of Chlamydomonas residues to those of tobacco. Whereas an aspartate 86 to arginine substitution had little effect, aspartate 94 to lysine Rubisco was only partially activated by spinach activase but now fully activated by tobacco activase. In an attempt to eliminate the activase/Rubisco interaction, proline 89 was changed to alanine, which is not present in either non-Solanaceae or Solanaceae Rubisco. This substitution also caused reversal of activase specificity, indicating that amino acid identity alone does not determine the specificity of the interaction.

* This work was supported in part by United States Department of Agriculture Grant 97-35306-4525 (to R. J. S.), Cooperative Regional Research Project NC-142 (to A. R. P. and R. J. S.), and Nebraska Agricultural Research Division undergraduate fellowships (to C. M. O. and B. D. S.). This is Nebraska Agricultural Research Division Journal Series Paper 13031.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Recipient of a Milton E. Mohr undergraduate scholarship. Present address: Dept. of Physiology, University of California, San Francisco, CA 94143.

Recipient of a Milton E. Mohr undergraduate scholarship. Present address: Dept. of Biochemistry, University of Wisconsin, Madison, WI 53706.

** To whom correspondence should be addressed. Tel.: 402-472-5446; Fax: 402-472-7842; E-mail: rspreitzer1@unl.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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