Primary structure of tektin Al: Comparison with intermediatefilament proteins and a model for its association with tubulin

J. M. Norrander, L. A. Amos, R. W. Linck

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36 Scopus citations

Abstract

Tektins are proteins that form filamentous polymers in the walls of ciliary and fiagellar 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 (Mr 52,955) is a series of α-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.

Original languageEnglish (US)
Pages (from-to)8567-8571
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number18
DOIs
StatePublished - 1992

Keywords

  • Basal body
  • Centriole
  • Cilia
  • Flagella
  • Microtubule

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