J. Biochem, 1993, Vol. 114, No. 4 453-456
© 1993 Japanese Biochemical Society
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Characterization of Wild Type and Mutant Chicken Gizzard 
Calponin Expressed in E. coli1
*Department of Muscle Research, Boston Biomedical Research Institute Boston, Massachusetts 02114, U.S.A.
**Department of Medicine, The Center for Adult Diseases Osaka, Osaka 537
***Laboratory of Cellular and Molecular Cardiology, Howard Hughs Medical Institute, Department of Cardiology, Children's Hospital, Harvard Medical School Boston, Massachusetts 02115, U.S.A.
****Department of Biochemistry, Tufts University School of Medicine Boston, Massachusetts 02111, U.S.A.
2To whom correspondence should be addressed at: Department of Muscle Research, Boston Biomedical Research Institute, 20 Staniford St., Boston, MA 02114, U.S.A.
Calponin is a thin filament-associated protein that is implicated in the regulation and maintenance of smooth muscle contraction. Molecular cloning of chicken gizzard calponin indicated the presence of two isoforms, 
and ß, the expression of the -isoform being uniformly more abundant in various smooth muscle tissues [Takahashi, E. & Nadal-Ginard, B. (1991) J. Biol. Chem. 266, 13284–13288]. For the long-range goal of understanding of the structure and function of calponin, we have started bacterial expression and site-directed mutagenesis of calponin. The amino acid composition and N-terminal sequence of the recombinant calponin were found to be identical to those deduced from its nucleotide sequence. Recombinant calponin is capable of binding to calmodulin, troponin C, tropomyosin, and actin, and of inhibiting skeletal muscle acto-subfragment-1 ATPase activity. A mutant calponin with a replacement in the putative inhibitory region (residues 146–171) has impaired ability to inhibit the acto-subfragment-1 ATPase activity, suggesting that this region of calponin may be involved in the modulation of the actin-myosin interactions.
1This work was supported by a Grant-in-Aid from the American Heart Association and with funds contributed in part by the AHA, Massachusetts Affiliate.
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