Characterization of an unusual tropoelastin with truncated C-terminus in the frog.
Tropoelastin is the monomeric form of elastin, a major polymeric protein of the extracellular elastic matrix of vertebrate tissues with properties of extensibility and elastic recoil. Mammalian and avian species contain a single gene for tropoelastin. A tropoelastin gene has also previously been identified in amphibians. In contrast, two tropoelastin genes with different tissue expression patterns have been described in teleosts. While general characteristics of tropoelastins, such as alternating arrangements of hydrophobic and crosslinking domains, are conserved across a wide phylogenetic range, sequences of these domains are highly variable, particularly when amphibian and teleost tropoelastins are included. For this reason exon-to-exon correspondence is not clear, and overall alignment of tropoelastin sequences across all species is not possible. An exception to this is the C-terminal exon, whose coding sequence has been very well-conserved across all species described to date. In mammalians this C-terminal domain has been shown to be important for interactions with cells and other matrix-associated proteins involved in matrix assembly. Here we identify and characterize a second tropoelastin gene in the frog with several unusual characteristics, the most striking of which is truncation of the C-terminal domain, deleting normally conserved sequence motifs. We demonstrate that, in spite of the absence of these motifs, both frog tropoelastin genes are expressed and incorporated into the elastic matrix, although with differential tissue localizations.
Miao
Ming
M
Molecular Structure and Function Program, Hospital for Sick Children, Toronto, Canada.
Stahl
Richard J
RJ
Petersen
Lars F
LF
Reintsch
Wolfgang E
WE
Davis
Elaine C
EC
Keeley
Fred W
FW
D000595:Amino Acid Sequence; D000818:Animals; D004549:Elastin / Q000235:genetics / Q000378:metabolism; D019143:Evolution, Molecular; D005091:Exons; D006801:Humans; D008168:Lung / Q000378:metabolism / Q000648:ultrastructure; D008969:Molecular Sequence Data; D010455:Peptides / Q000235:genetics / Q000378:metabolism; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012867:Skin / Q000378:metabolism / Q000648:ultrastructure; D014333:Tropoelastin / Q000235:genetics / Q000378:metabolism*; D014981:Xenopus / Q000378:metabolism*; D029867:Xenopus Proteins / Q000235:genetics / Q000378:metabolism*
D010455:Peptides; D020033:Protein Isoforms; D014333:Tropoelastin; D029867:Xenopus Proteins; D004549:Elastin