An Sfi1p-Like Centrin-Binding Protein Mediates Centrin-Based Ca
2+
-Dependent Contractility in
Paramecium tetraurelia
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Published:2007-11
Issue:11
Volume:6
Page:1992-2000
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ISSN:1535-9778
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Container-title:Eukaryotic Cell
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language:en
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Short-container-title:Eukaryot Cell
Author:
Gogendeau Delphine123, Beisson Janine123, de Loubresse Nicole Garreau123, Le Caer Jean-Pierre4, Ruiz Françoise123, Cohen Jean123, Sperling Linda123, Koll France123, Klotz Catherine123
Affiliation:
1. Centre de Génétique Moléculaire, UPR 2167 2. Université Paris-Sud, F-91405 Orsay 3. Université Pierre et Marie Curie, Paris 6, F-75005 Paris, France 4. Institut de Chimie des Substances Naturelles, UPR 2301, CNRS, F-91198 Gif-sur-Yvette
Abstract
ABSTRACT
The previous characterization and structural analyses of Sfi1p, a
Saccharomyces cerevisiae
centrin-binding protein essential for spindle pole body duplication, have suggested molecular models to account for centrin-mediated, Ca
2+
-dependent contractility processes (S. Li, A. M. Sandercock, P. Conduit, C. V. Robinson, R. L. Williams, and J. V. Kilmartin, J. Cell Biol. 173:867-877, 2006). Such processes can be analyzed by using
Paramecium tetraurelia
, which harbors a large Ca
2+
-dependent contractile cytoskeletal network, the infraciliary lattice (ICL). Previous biochemical and genetic studies have shown that the ICL is composed of diverse centrin isoforms and a high-molecular-mass centrin-associated protein, whose reduced size in the démaillé (dem1) mutant correlates with defective organization of the ICL. Using sequences derived from the high-molecular-mass protein to probe the
Paramecium
genome sequence, we characterized the Pt
CenBP1
gene, which encodes a 460-kDa protein. PtCenBP1p displays six almost perfect repeats of ca. 427 amino acids (aa) and harbors 89 potential centrin-binding sites with the consensus motif LLX
11
F/LX
2
WK/R, similar to the centrin-binding sites of ScSfi1p. The smaller (260-kDa) protein encoded by the dem1 mutant Pt
CenBP1
allele comprises only two repeats of 427 aa and 46 centrin-binding sites. By using RNA interference and green fluorescent protein fusion experiments, we showed that PtCenBP1p forms the backbone of the ICL and plays an essential role in its assembly and contractility. This study provides the first in vivo demonstration of the role of Sfi1p-like proteins in centrin-mediated Ca
2+
-dependent contractile processes.
Publisher
American Society for Microbiology
Subject
Molecular Biology,General Medicine,Microbiology
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