Work

Primary structure of tektin A1: comparison with intermediate-filament proteins and a model for its association with tubulin.

Year: 1992

Type: article

Abstract: Tektins are proteins that form filamentous polymers in the walls of ciliary and flagellar microtubules and that have biochemical and immunological properties similar to those of intermediate-filament proteins. We report here the sequence of a cDNA for tektin A1, one of the main tektins from Strongylocentrotus purpuratus sea urchin embryos. By hybridization analysis, tektin A mRNA appears maximally at ciliogenesis. The predicted structure of tektin A1 (M(r) 52,955) is a series of alpha-helical rod segments separated by nonhelical linkers. The two halves of the rod appear homologous and are probably related by gene duplication. Comparison of tektin A1 with intermediate-filament proteins, including nuclear lamins, reveals a low amino acid homology but similar molecular motif, i.e., pattern of helical and nonhelical domains. This study indicates that tektins are unique proteins but may be evolutionarily related to intermediate-filament proteins, and suggests a structural basis for the interaction of tektins and tubulin in microtubules.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.89.18.8567

Authors: J M Norrander, L A Amos, R W Linck

Institutions: University of Minnesota, Medical Research Council

Language: English

Topic: Genetic and Kidney Cyst Diseases

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: MOLECULAR GENETICS OF TEKTIN PROTEINS, G1895183371, MOLECULAR BIOLOGY OF FLAGELLA AND BASAL BODIES, G8816798635