Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence.

Abstract

The nucleotide sequence of 2 recombinant plasmids (pBR 322) containing hamster vimentin cDNA [complementary DNA] was determined. The sequence comprises, 1640 base pairs and reveals virtually the total primary structure of vimentin and a large part of the 3'' noncoding region. Secondary structure prediction methods allow the characterization of 2 distinct regions of the polypeptide chain, 135 and 145 residues long, which are able to form .alpha. helices organized in coiled coils. Three nonhelical domains can be distinguished: a very basic NH2-terminal domain of at least 67 residues, a nonhelical region of 45 amino acids separating the 2 helix domains and a COOH-terminal region of 55 residues, which contains an excess of acidic amino acids. The meaning of each of these domains of the vimentin polypeptide for the subunit and filament formation is discussed.