title: Calcium-calmodulin suppresses the filamentous actin-binding activity of a 135-kilodalton actin-bundling protein isolated from lily pollen tubes.
abstract: We have isolated a 135-kD actin-bundling protein (P-135-ABP) from lily (Lilium longiflorum) pollen tubes and have shown that this protein is responsible for bundling actin filaments in lily pollen tubes (E. Yokota, K. Takahara, T. Shimmen [1998] Plant Physiol 116: 1421-1429). However, only a few thin actin-filament bundles are present in random orientation in the tip region of pollen tubes, where high concentrations of Ca(2+) have also been found. To elucidate the molecular mechanism for the temporal and spatial regulation of actin-filament organization in the tip region of pollen tubes, we explored the possible presence of factors modulating the filamentous actin (F-actin)-binding activity of P-135-ABP. The F-actin-binding activity of P-135-ABP in vitro was appreciably reduced by Ca(2+) and calmodulin (CaM), although neither Ca(2+) alone nor CaM in the presence of low concentrations of Ca(2+) affects the activity of P-135-ABP. A micromolar order of Ca(2+) and CaM were needed to induce the inhibition of the binding activity of P-135-ABP to F-actin. An antagonist for CaM, W-7, cancelled this inhibition. W-5 also alleviated the inhibition effect of Ca(2+)-CaM, however, more weakly than W-7. These results suggest the specific interaction of P-135-ABP with Ca(2+)-CaM. In the presence of both Ca(2+) and CaM, P-135-ABP organized F-actin into thin bundles, instead of the thick bundles observed in the absence of CaM. These results suggest that the inhibition of the P-135-ABP activity by Ca(2+)-CaM is an important regulatory mechanism for organizing actin filaments in the tip region of lily pollen tubes.
authors.affiliation: Department of Life Science, Himeji Institute of Technology, Harima Science Park City, Hyogo, Japan. yokota@sci.himeji-tech.ac.jp
authors.forename: E
authors.initials: E
authors.lastname: Yokota
authors.forename: S
authors.initials: S
authors.lastname: Muto
authors.forename: T
authors.initials: T
authors.lastname: Shimmen
mesh_terms: D000199:Actins / Q000378:metabolism*; D002147:Calmodulin / Q000037:antagonists & inhibitors / Q000502:physiology*; D019668:Liliaceae / Q000737:chemistry*; D008840:Microfilament Proteins / Q000302:isolation & purification / Q000378:metabolism*; D011058:Pollen / Q000737:chemistry*; D011485:Protein Binding
chemical_list: D000199:Actins; D002147:Calmodulin; D008840:Microfilament Proteins; C052523:actin filament bundling proteins