Volume 46, Issue 5 pp. 469-472
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Actin of Histriculus cavicola: Characteristics of the Highly Divergent Hypotrich Ciliate Actins1

PILAR PÉREZ-ROMERO

PILAR PÉREZ-ROMERO

Departamento de Microbiología. Facultad de Biología. Universidad de Sevilla. Apdo. 1095. 41080, Spain

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EDUARDO VILLALOBO

EDUARDO VILLALOBO

Departamento de Microbiología. Facultad de Biología. Universidad de Sevilla. Apdo. 1095. 41080, Spain

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CORÍN DÍAZ-RAMOS

CORÍN DÍAZ-RAMOS

Departamento de Microbiología. Facultad de Biología. Universidad de Sevilla. Apdo. 1095. 41080, Spain

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PURIFICACIÓN CALVO

PURIFICACIÓN CALVO

Departamento de Microbiología. Facultad de Biología. Universidad de Sevilla. Apdo. 1095. 41080, Spain

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ANTONIO TORRES

ANTONIO TORRES

Departamento de Microbiología. Facultad de Biología. Universidad de Sevilla. Apdo. 1095. 41080, Spain

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First published: 14 May 2007
Citations: 9
Corresponding Author: A. Torres—Telephone number: 34-954557115; FAX number: 34-954557830; Email: [email protected]
1

The nucleotide sequence of the H. cavicola actin gene is available in the EMBL data base under the accession number Y12047.

ABSTRACT

A macronuclear gene-sized molecule carrying an actin gene from the hypotrich ciliate, Histriculus cavicola, was characterized. Southern blot analysis using a coding region probe suggested that actin in H. cavicola is encoded by a single gene. A comparison of the promoter regions indicated that the H. cavicola actin gene has a TATA box in the 51 flanking region in a position identical to those in other oxytrich ciliates. The coding sequence of this gene is not interrupted by any introns, and codes for a protein of 375 amino acid residues. This protein shares a high degree of similarity with other oxytrichid actins, and a relatively low similarity with actins from other eukaryotes. Comparative analyses of sequences indicated that most of the amino acid substitutions in hypotrich actins are found in surface loops, while the core structures are well-conserved. The sites that interact with DNase I and several regions involved in actin-actin contact have diverged considerably in hypotrich actins, while nucleotide-binding sites are the best-conserved interaction motif.

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