Effects of post-translational modifications catalysed by pollen transglutaminase on the functional properties of microtubules and actin filaments

DEL, D., SERAFINI-FRACASSINI, D., BONNER, P.L.R., CRESTI, M. and CAI, G., 2009. Effects of post-translational modifications catalysed by pollen transglutaminase on the functional properties of microtubules and actin filaments. Biochemical Journal, 418, pp. 651-664.

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Abstract

TGases (transglutaminases) are a class of calcium-dependent enzymes that catalyse the interactions between acyl acceptor glutamyl residues and amine donors, potentially making crosslinks between proteins. To assess the activity of apple (Malus domestica) pollen TGase on the functional properties of actin and tubulin, TGase was prepared from apple pollen by hydrophobic interaction chromatography and assayed on actin and tubulin purified from the same cell type. The enzyme catalysed the incorporation of putrescine in the cytoskeleton monomers. When tested on actin filaments, pollen TGase induced the formation of high-molecular-mass aggregates of actin. Use of fluorescein– cadaverine showed that the labelled polyamine was incorporated into actin by pollen TGase, similar to with guinea pig liver TGase. The pollen TGase also reduced the enzyme activity and the binding of myosin to TGase-treated actin filaments. Polymerization of tubulin in the presence of pollen TGase also yielded the formation of high molecular mass aggregates. Furthermore, the pollen TGase also affected the binding of kinesin to microtubules and reduced the motility of microtubules along kinesincoated slides. These results indicate that the pollen tube TGase can control different properties of the pollen tube cytoskeleton (including the ability of actin and tubulin to assemble and their interaction with motor proteins) and consequently regulate the development of pollen tubes.

Item Type: Journal article
Description: The final version of record is available at http://www.biochemj.org/bj/default.htm
Publication Title: Biochemical Journal
Creators: Del, D., Serafini-Fracassini, D., Bonner, P.L.R., Cresti, M. and Cai, G.
Publisher: Portland Press
Date: 2009
Volume: 418
Divisions: Schools > School of Science and Technology
Depositing User: EPrints Services
Date Added: 09 Oct 2015 09:43
Last Modified: 09 Jun 2017 13:09
URI: http://irep.ntu.ac.uk/id/eprint/1682

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