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Primary structure of the kinase domain region of rabbit skeletal and cardiac muscle titin. J Muscle Res Cell Motil 1996 Jun;17(3):343-8

Date

06/01/1996

Pubmed ID

8814553

DOI

10.1007/BF00240931

Abstract

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.

Author List

SebestyƩn MG, Fritz JD, Wolff JA, Greaser ML

Author

Jeffery Duane Fritz PhD Associate Professor in the Medical School Regional Campuses department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Animals
Binding Sites
Caenorhabditis elegans
Calmodulin-Binding Proteins
Chickens
Connectin
Humans
Molecular Sequence Data
Muscle Proteins
Muscle, Skeletal
Myocardium
Myosin-Light-Chain Kinase
Oligonucleotides, Antisense
Protein Kinases
RNA, Messenger
Rabbits
Ribonuclease H
Sequence Homology, Amino Acid