Expression in Escherichia coli and a functional study of a beta-troponin T 25 kDa fragment of rabbit skeletal muscle.
A 25 kDa fragment of beta-type troponin T (beta-TnT) was expressed in Escherichia coli, and its function as a component of the regulatory system for actomyosin ATPase was compared with that of the authentic counterpart, the full length alpha-TnT. The expressed species, designated as beta-TnT(N'-208), consists of 208 residues. It lacks the entire variable region at the amino-terminus and, near the carboxyl-terminus, a segment of 14 residues is changed from the alpha-type to the beta-type sequence. Functional tests indicated that the truncated beta-TnT was not distinguishable from the full length alpha-TnT, suggesting that neither deletion of the variable N-terminal region nor alteration of the type has a significant effect on the regulatory action of TnT.
Fujita
S
S
European Molecular Biology Laboratory, DESY, Hamburg, Germany.
Maeda
K
K
Maéda
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004247:DNA / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics*; D015870:Gene Expression; D008969:Molecular Sequence Data; D009132:Muscles / Q000378:metabolism; D009218:Myosins / Q000378:metabolism; D010446:Peptide Fragments / Q000235:genetics* / Q000378:metabolism; D010957:Plasmids; D011817:Rabbits; D014336:Troponin / Q000235:genetics* / Q000378:metabolism; D020107:Troponin T
D010446:Peptide Fragments; D014336:Troponin; D020107:Troponin T; D004247:DNA; D009218:Myosins