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GTPase Activity and Biochemical Characterization of a Recombinant Cotton Fiber Annexin1

Heungsop Shin and R. Malcolm Brown Jr.*

Department of Botany, University of Texas, Austin, Texas, 78713-7640

A cDNA encoding annexin was isolated from a cotton (Gossypium hirsutum) fiber cDNA library. The cDNA was expressed in Escherichia coli, and the resultant recombinant protein was purified. We then investigated some biochemical properties of the recombinant annexin based on the current understanding of plant annexins. An "add-back experiment" was performed to study the effect of the recombinant annexin on beta -glucan synthase activity, but no effect was found. However, it was found that the recombinant annexin could display ATPase/GTPase activities. The recombinant annexin showed much higher GTPase than ATPase activity. Mg2+ was essential for these activities, whereas a high concentration of Ca2+ was inhibitory. A photolabeling assay showed that this annexin could bind GTP more specifically than ATP. The GTP-binding site on the annexin was mapped into the carboxyl-terminal fourth repeat of annexin from the photolabeling experiment using domain-deletion mutants of this annexin. Northern-blot analysis showed that the annexin gene was highly expressed in the elongation stages of cotton fiber differentiation, suggesting a role of this annexin in cell elongation.

1   This work was supported in part by grant no. DE-FG03-94ER20145 from the Division of Energy Biosciences, Department of Energy, and funds from the Johnson & Johnson Centennial Chair to R.M.B.
*   Corresponding author; e-mail rmbrown{at}mail.utexas.edu; fax 1-512-471-3573.

Plant Physiol. (1999) 119: 925-934
Copyright Clearance Center:   0032-0889/99/119//10
© 1999 American Society of Plant Physiologists




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