Primary structure of the kinase domain region of rabbit skeletal and cardiac muscle titin

✍ Scribed by Magdolna G. Sebestyén; Jeffery D. Fritz; Jon A. Wolff; Marion L. Greaser

• Publisher: Springer Netherlands
• Year: 1996
• Tongue: English
• Weight: 743 KB
• Volume: 17
• Category: Article
• ISSN: 0142-4319
• DOI: 10.1007/bf00240931

✦ Synopsis

A 2.3 kb region of rabbit cardiac and skeletal muscle titin has been cloned. The cDNA sequences of the two tissues are identical and show 91% identity on the nucleotide level with the corresponding region of human cardiac muscle titin. On the amino acid level the identity is 96% and similarity is 98%. Alignment of predicted amino acid sequences of several homologous kinase domains reveals that the rabbit titin kinase has all the necessary elements of an active catalytic domain and carries a potential regulatory region on its C-terminal end. The distance of the 2.3 kb contig from the 3' end of the message was determined to be 5.7 kb in both tissues using oligonucleotide directed RNase H cleavage of titin mRNAs. This is essentially identical with the length of the fully sequenced human cardiac titin C-terminal end. It therefore appears unlikely that there are major tissue specific differences in this 8 kb cDNA region which encodes the C-terminus of rabbit skeletal and cardiac titin.