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J. Biol. Chem., Vol. 262, Issue 17, 8112-8120, Jun, 1987
ZE Zehner, Y Li, BA Roe, BM Paterson and CM Sax
Here we report the nucleotide sequence of the chicken vimentin gene and its
deduced primary amino acid sequence. A comparison of this gene to other
intermediate filament protein genes demonstrates that both exon size and
position are strongly conserved features of this multigene family. In
addition, the hamster and chicken vimentin genes exhibit strong identity at
the level of nucleotide (74%) and amino acid (80%) sequence. Interestingly,
40% of total sequence diversity is localized to the N terminus or "head"
region of these genes whereas other protein domains (rod and C terminus)
are remarkably identical in both nucleotide (81%) and amino acid (89%)
sequence. Even stronger amino acid identity (100%) is exhibited in certain
subdomains which may define regions crucial for filament formation and
function. Not surprisingly, vimentin is more homologous across animal
species than it is to other intermediate filament protein members (e.g.
desmin) within the same species. A comparison of 5'-flanking sequences of
the hamster and chicken genes as well as other characterized promoter
elements (SV40, HSV-TK) reveals homologous sequence elements which may
define common and/or unique sites involved in the modulation of gene
expression. The implications of these sequence elements for both tissue-
specific and developmental expression of the vimentin gene are discussed.
The chicken vimentin gene. Nucleotide sequence, regulatory elements, and comparison to the hamster gene
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