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Equus caballus gelsolin - cDNA sequence and protein structural implications

TitleEquus caballus gelsolin - cDNA sequence and protein structural implications
Publication TypeJournal Article
Year of Publication1998
AuthorsKoepf, EK, Hewitt, J, Vo, H, MacGillivray, RTA, Burtnick, LD
JournalEuropean Journal of Biochemistry
Date PublishedFeb
Type of ArticleArticle
ISBN Number0014-2956
Keywordsactin-binding protein, ACTIN-SEVERING PROTEINS, amino acid sequence, AMPLIFICATION, BINDING DOMAIN, cDNA sequence, CLONING, CYTOPLASMIC FORMS, DNA, END, extraction, gelsolin, HORSE PLASMA GELSOLIN, MUSCLE, protein structure

We have generated and characterized the cDNA from equine smooth muscle that Encodes gelsolin, an actin-modulating protein. Overlapping cDNA clones synthesized by the reverse transcriptaseoplymerase chain reaction and clones isolated from a horse genomic library provided the complete primary structure for the intracellular isoform of gelsolin, while cDNA complemented with protein sequence data produced the full-length primary transcript of the gelsolin isoform found circulating in equine plasma. The deduced amino acid sequences of the intracellular and secreted versions of equine gelsolin infer polypeptides of 731 and 755 residues with apparent molecular masses of 80.7 kDa and 83.2 kDa, respectively. Multiple sequence alignment analysis of equine, human, porcine, and murine orthologs of gelsolin demonstrates prominent similarities among all of these proteins, with the horse and human molecules exhibiting the largest degree of likeness with respect to polypeptide length and overall sequence composition. Both horse and human plasma gelsolins are comprised of 755 amino acids with 94% of the residues identical, while the degree of sequence identity in the shorter (731 residues) cytoplasmic gelsolins is 95 %. Analysis of the sequences and structures of the six related domains that comprise gelsolin emphasizes the strong correlation that exists between primary structural conservation among mammalian gelsolins and maintenance of the three-dimensional domain fold characteristic of members of this protein family.

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