Genetic evidence for a role of centrin-associated proteins in the organization and dynamics of the infraciliary lattice in Paramecium

• Published in: Cell motility and the cytoskeleton Vol. 38; no. 2; p. 172
• Main Authors: Klotz, C, Garreau de Loubresse, N, Ruiz, F, Beisson, J
• Format: Journal Article
• Language: English
• Published: United States 1997
• Subjects: Animals; Calcium-Binding Proteins - genetics; Calcium-Binding Proteins - metabolism; Centrosome - metabolism; Chromosomal Proteins, Non-Histone; Cilia - chemistry; Cilia - genetics; Cilia - ultrastructure; Contractile Proteins - genetics; Contractile Proteins - metabolism; Fluorescent Antibody Technique, Indirect; Microscopy, Immunoelectron; Mutation; Paramecium
• ISSN: 0886-1544; 1097-0169
• DOI: 10.1002/(SICI)1097-0169(1997)38:2<172::AID-CM6>3.0.CO;2-9

Within the superfamily of "EF-hand Ca2+-modulated proteins," centrins constitute a family of cytoskeletal proteins that are highly conserved from lower eukaryotes to man. Their cytoskeletal specialization is manifest in their capacity to form filamentous contractile arrays of various shapes and functions and by their association with microtubule organizing centres (MTOCs). While the latter property has been conserved throughout the evolution of eukaryotes, centrin-based contractile structures are only found in protists where they form arrays of widely diverse organization and function. In the ciliate Paramecium tetraurelia, three centrin genes have been characterized, which may be part of a larger centrin gene family [Madeddu et al., 1996: Eur J. Biochem. 238:121-128]. The products of these genes were originally identified as components of the infraciliary lattice, a contractile cytoskeletal network [Garreau de Loubresse et al., 1991: Biol. Cell 71:217-225]. We show here that centrins are localized not only in this lattice but also in basal bodies and in the cord, a filamentous structure associated with the oral apparatus. We demonstrate that in the infraciliary lattice, but not in basal bodies, centrins are associated with high-molecular-weight proteins (ca. 350 kD). Their role in the biogenesis of the infraciliary lattice is documented by cytological and biochemical properties of the mutant "démaillé" (dem1) characterized by altered centrin-associated proteins and abnormal organization and dynamics of the infraciliary lattice.