Showing papers by "Charles P. Ordahl published in 1986"
TL;DR: There is evidence that the fast skeletal isoform of the chick troponin I (sTnI) protein has been sequenced and its organization into exons and introns established, and a comparison of nucleotide sequence in the 5' flanking region of several muscle-specific genes reveals a heptanucleotide consensus sequence, 5'-CATTCCT-3'.
Abstract: The gene encoding the fast skeletal isoform of the chick troponin I (sTnI) protein has been sequenced and its organization into exons and introns established. The gene is approximately 4.5 kb in length and composed of 8 exons, the first of which contains solely 5' untranslated sequence. In addition to its major mRNA product, there is evidence that the sTnI gene encodes a second mRNA, present at low abundance levels in embryonic skeletal muscle. Sl nuclease protection and primer extension experiments indicate that the low abundance mRNA is initiated approximately 47 nucleotides upstream of the major transcriptional initiation site. Both mRNAs appear to encode identical sTnI polypeptides. A comparison of nucleotide sequence in the 5' flanking region of several muscle-specific genes, including the sTnI gene, reveals a heptanucleotide consensus sequence, 5'-CATTCCT-3', which is conserved in the 5' flanking regions of many vertebrate contractile protein genes.
69 citations
TL;DR: Results for early embryonic Striated muscle indicate that both genes are coexpressed throughout striated muscle ontogeny and may not be regulated under unique tissue-specific regulatory programs but each may have acquired regulatory elements which confer important quantitative differences in their level of expression in maturestriated muscle cells.
66 citations
TL;DR: Preliminary secondary structural predictions suggest that the C-terminal half of the protein is likely an α/β-type protein and placement in the sequence of two peptides found in previous cross-linking studies reveals two stretches of primary structure that are presumably close in space to the reactive Cys-283 and hence close to the active site.
Abstract: Comparisons of nine creatine kinase sequences show that 67% of the protein sequence is identical among rabbit, rat, mouse, and chicken muscle, rabbit, rat, and chicken brain, and electric organ sequences from two species of electric ray(Torpedo). The extensive homology precludes a facile prediction of active-site residues based on sequence conservation. The sequences are more similar within isozyme types than are the different isozymes from any one species. There are 35 positions in the muscle and brain sequence pairs for three species which differentiate the two forms. TheTorpedo sequences do not fall completely into either of these patterns. Except for homology with partial sequences of other ATP-guanidino phosphotransferases, no significant homology with other protein or nucleic acid sequences in available databases was found. Preliminary secondary structural predictions suggest that the C-terminal half of the protein is likely an α/β-type protein. Placement in the sequence of two peptides found in previous cross-linking studies reveals two stretches of primary structure that are presumably close in space to the reactive Cys-283 and hence close to the active site.
43 citations
1 citations