The discovery of delta-tubulin, the fourth member of the tubulin superfamily, in Chlamydomonas [1] has led to the identification in the genomes of vertebrates and protozoa of putative delta homologues and of additional tubulins, epsilon and zeta [2-4]. These discoveries raise questions concerning the functions of these novel tubulins, their interactions with microtubule arrays and microtubule-organising centres, and their evolutionary status. The sm19-1 mutation of Paramecium specifically inhibits basal body duplication [5] and causes delocalisation of gamma-tubulin, which is also required for basal body duplication [6]. We have cloned the SM19 gene by functional complementation and found that it encodes another new member of the tubulin superfamily. SM19p, provisionally called eta-tubulin (eta-tubulin), shows low sequence identity with the tubulins previously identified in Paramecium, namely, alpha [7], beta [8], gamma [6], delta (this work) and epsilon (P. Dupuis-Williams, personal communication). Phylogenetic analysis indicated that SM19p is not consistently grouped with any phylogenetic entity.

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SummaryIn this study, we report cloning, by functional complementation of the KIN241 gene involved in Paramecium cell morphogenesis, cortical organization and nuclear reorganization. This gene is predicted to encode a protein of a novel type, comprising a cyclophilin-type, peptidyl-prolyl isomerase domain, an RNA recognition motif, followed by a region rich in glutamate and lysine (EK domain) and a C-terminal string of serines. As homologues of this protein are present in the genomes of Schizosaccharomyces pombe, Caenorhabditis elegans, Drosophila melanogaster, Arabidopsis thaliana and Homo sapiens, the Kin241p predicted sequence defines a new family of proteins that we propose to call 'CRIP', for cyclophilin-RNA interacting protein. We demonstrate that, in Paramecium, Kin241p is localized in the nucleus and that deletion of some nuclear localization signals (NLSs) decreases transport of the protein into the nucleus. No Kin241-1 protein is present in mutant cells, suggesting that the C-terminal serine-rich region is responsible for protein stability.