Isolation and sequence of a tropomyosin-binding fragment of turkey gizzard calponin.
Limited chymotryptic cleavage of turkey gizzard calponin yields a 13 kDa fragment which could be purified by its ability to bind to Sepharose-immobilized tropomyosin. This 13 kD polypeptide is shown to be derived from a 22 kDa fragment. Complete amino acid sequence analysis of the 13 kD and 22 kD fragments reveals high homology with the formerly characterized smooth muscle-specific protein SM22 alpha (Pearlstone, J.R., Weber, M., Lees-Miller, J.P., Carpenter, M.R. and Smillie L.B., 1987, J. Biol. Chem. 262, 5985-5991) and the product of gene mp20 of Drosophila (Ayme-Southqate, A., Lasko, P., French, C, and Pardue, M.L. [(1989) J. Cell Biol. 108, 521-531]. Futhermore we recognize sequence elements of a putative actin-binding domain of alpha-actinin, the calpactin I or p 36 sequence, and a consensus motif present in the repeats of the gene product of the candidate unc-87 gene of C. elegans (S.D. Goetinck and R.H. Waterston, personal communication).
Vancompernolle
K
K
Laboratory of Physiological Chemistry, Gent, Belgium.
Gimona
M
M
Herzog
M
M
Van Damme
J
J
Vandekerckhove
J
J
Small
V
V
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002135:Calcium-Binding Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D005895:Gizzard, Avian / Q000378:metabolism; D008840:Microfilament Proteins; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000378:metabolism*; D009130:Muscle, Smooth / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid; D014335:Tropomyosin / Q000378:metabolism; D014422:Turkeys; D000096985:Calponins
D002135:Calcium-Binding Proteins; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D008840:Microfilament Proteins; D009124:Muscle Proteins; D010446:Peptide Fragments; D014335:Tropomyosin; D000096985:Calponins