Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1977 Feb 1;161(2):371–382. doi: 10.1042/bj1610371

The phosphorylation sites of troponin T from white skeletal muscle and the effects of interaction with troponin C on their phosphorylation by phosphorylase kinase.

A J Moir, H A Cole, S V Perry
PMCID: PMC1164514  PMID: 849266

Abstract

1. The phosphorylation of troponin T from rabbit white sketetal muscle is catalysed by phosphorylase kinase, but not at a significant rate by bovine 3':5'-cyclic AMP-dependent protein kinase. 2. The amino acid sequences adjacent to the three major phosphorylation sites of troponin T were determined. 3. The serine in the N-terminal peptide (Asx,SerP, Glx)Glu-Val-Glu, is that phosphorylated (SerP, phosphoserine) when the troponin complex is isolated. 4. The other two sites of phosphorylation are located in the sequence Ala-Leu-(Ser, SerP)-Met-Gly-Ala-Asn-Tyr(Ser,SerP)Tyr. 5. When troponin T is phosphorylated in the presence of troponin C, the extent of phosphorylation at each site is considerably decreased. 6. CNBr fragments of troponin T are also phosphorylated by phosphorylase kinase, but the rate of phosphorylation at each site in the CNBr fragments is considerably slower than in the native protein. 7. From these studies it is suggested that troponin C interacts with troponin T in the region containing the two closely situated phosphorylation sites.

Full text

PDF
382

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Cohen P. The subunit structure of rabbit-skeletal-muscle phosphorylase kinase, and the molecular basis of its activation reactions. Eur J Biochem. 1973 Apr 2;34(1):1–14. doi: 10.1111/j.1432-1033.1973.tb02721.x. [DOI] [PubMed] [Google Scholar]
  2. Cole H. A., Perry S. V. The phosphorylation of troponin I from cardiac muscle. Biochem J. 1975 Sep;149(3):525–533. doi: 10.1042/bj1490525. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ebashi S., Wakabayashi T., Ebashi F. Troponin and its components. J Biochem. 1971 Feb;69(2):441–445. doi: 10.1093/oxfordjournals.jbchem.a129486. [DOI] [PubMed] [Google Scholar]
  4. Gross S. R., Mayer S. E. The phosphorylation of troponin B by phosphorylase b kinase in skeletal muscle of mice carrying the phosphorylase b kinase deficiency gene. Biochem Biophys Res Commun. 1973 Sep 18;54(2):823–830. doi: 10.1016/0006-291x(73)91498-8. [DOI] [PubMed] [Google Scholar]
  5. HEILMANN J., BARROLLIER J., WATZKE E. Beitrag zur Aminosäurebestimmung auf Papierchromatogrammen. Hoppe Seylers Z Physiol Chem. 1957;309(4-6):219–220. [PubMed] [Google Scholar]
  6. Hartley B. S. Strategy and tactics in protein chemistry. Biochem J. 1970 Oct;119(5):805–822. doi: 10.1042/bj1190805f. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Huang T. S., Bylund D. B., Stull J. T., Krebs E. G. The amino acid sequences of the phosphorylated sites in troponin-I from rabbit skeletal muscle. FEBS Lett. 1974 Jun 15;42(3):249–252. doi: 10.1016/0014-5793(74)80738-6. [DOI] [PubMed] [Google Scholar]
  8. Jackson P., Amphlett G. W., Perry S. V. The primary structure of troponin T and the interaction with tropomyosin. Biochem J. 1975 Oct;151(1):85–97. doi: 10.1042/bj1510085. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Moir A. J., Wilkinson J. M., Perry S. V. The phosphorylation sites of troponin I from white skeletal muscle of the rabbit. FEBS Lett. 1974 Jun 15;42(3):253–256. doi: 10.1016/0014-5793(74)80739-8. [DOI] [PubMed] [Google Scholar]
  10. NOLAN C., NOVOA W. B., KREBS E. G., FISCHER E. H. FURTHER STUDIES ON THE SITE PHOSPHORYLATED IN THE PHOSPHORYLASE B TO A REACTION. Biochemistry. 1964 Apr;3:542–551. doi: 10.1021/bi00892a013. [DOI] [PubMed] [Google Scholar]
  11. Pearlstone J. R., Carpenter M. R., Johnson P., Smillie L. B. Amino-acid sequence of tropomyosin-binding component of rabbit skeletal muscle troponin. Proc Natl Acad Sci U S A. 1976 Jun;73(6):1902–1906. doi: 10.1073/pnas.73.6.1902. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Perry S. V., Cole H. A. Phosphorylation of the "37000 component" of the troponin complex (troponin-t). Biochem J. 1973 Feb;131(2):425–428. doi: 10.1042/bj1310425. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Perry S. V., Cole H. A. Phosphorylation of troponin and the effects of interactions between the components of the complex. Biochem J. 1974 Sep;141(3):733–743. doi: 10.1042/bj1410733. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Pratje E., Heilmeyer L. M.G. Phosphorylation of rabbit muscle troponin and actin by a 3', 5'-c-AMP-dependent protein kinase. FEBS Lett. 1972 Oct 15;27(1):89–93. doi: 10.1016/0014-5793(72)80416-2. [DOI] [PubMed] [Google Scholar]
  15. Syska H., Wilkinson J. M., Grand R. J., Perry S. V. The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit. Biochem J. 1976 Feb 1;153(2):375–387. doi: 10.1042/bj1530375. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Van Eerd J. P., Kawasaki Y. Effect of calcium(II) on the interaction between the subunits of troponin and tropomyosin. Biochemistry. 1973 Nov 20;12(24):4972–4980. doi: 10.1021/bi00748a024. [DOI] [PubMed] [Google Scholar]
  17. Wilkinson J. M. The preparation and properties of the components of troponin B. Biochim Biophys Acta. 1974 Aug 8;359(2):379–388. doi: 10.1016/0005-2795(74)90238-4. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES