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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1984 Jun;81(12):3685–3689. doi: 10.1073/pnas.81.12.3685

Titin is an extraordinarily long, flexible, and slender myofibrillar protein.

K Wang, R Ramirez-Mitchell, D Palter
PMCID: PMC345283  PMID: 6587383

Abstract

" Titin " is a term used to describe a pair of closely related megadalton polypeptides that together are the third most abundant myofibrillar protein in a wide range of striated muscles. It has been proposed that titin and another giant protein, nebulin , are the major components of an elastic cytoskeletal lattice within the sarcomere. We have now purified the leading band, titin -2 (T2), of the titin doublet in native forms by extraction with Guba -Straub solution followed by chromatography. Electron microscopy of low-angle-shadowed and negatively stained specimens revealed that T2 chains self-assembled into extremely long (from 0.1 micron to over 1.0 micron), flexible, and extensible slender strands (4-5 nm in diameter) with axial periodicity. Furthermore, these strands tended to associate to form filamentous bundles and meshworks. Thus, titin appears to be ideally suited as a component of an elastic lattice that serves as an organizing scaffold or template for thick and thin filaments.

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Selected References

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  1. Erickson H. P., Carrell N., McDonagh J. Fibronectin molecule visualized in electron microscopy: a long, thin, flexible strand. J Cell Biol. 1981 Dec;91(3 Pt 1):673–678. doi: 10.1083/jcb.91.3.673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. HUXLEY H. E. ELECTRON MICROSCOPE STUDIES ON THE STRUCTURE OF NATURAL AND SYNTHETIC PROTEIN FILAMENTS FROM STRIATED MUSCLE. J Mol Biol. 1963 Sep;7:281–308. doi: 10.1016/s0022-2836(63)80008-x. [DOI] [PubMed] [Google Scholar]
  3. Heuser J. E. Procedure for freeze-drying molecules adsorbed to mica flakes. J Mol Biol. 1983 Sep 5;169(1):155–195. doi: 10.1016/s0022-2836(83)80179-x. [DOI] [PubMed] [Google Scholar]
  4. Kimura S., Maruyama K. Preparation of native connectin from chicken breast muscle. J Biochem. 1983 Dec;94(6):2083–2085. doi: 10.1093/oxfordjournals.jbchem.a134569. [DOI] [PubMed] [Google Scholar]
  5. Locker R. H., Leet N. G. Histology of highly-stretched beef muscle. I. The fine structure of grossly stretched single fibers. J Ultrastruct Res. 1975 Jul;52(1):64–75. doi: 10.1016/s0022-5320(75)80022-0. [DOI] [PubMed] [Google Scholar]
  6. Offer G., Moos C., Starr R. A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization. J Mol Biol. 1973 Mar 15;74(4):653–676. doi: 10.1016/0022-2836(73)90055-7. [DOI] [PubMed] [Google Scholar]
  7. Starr R., Offer G. Preparation of C-protein, H-protein, X-protein, and phosphofructokinase. Methods Enzymol. 1982;85(Pt B):130–138. doi: 10.1016/0076-6879(82)85016-7. [DOI] [PubMed] [Google Scholar]
  8. Trinick J. A. End-filaments: a new structural element of vertebrate skeletal muscle thick filaments. J Mol Biol. 1981 Sep 15;151(2):309–314. doi: 10.1016/0022-2836(81)90517-9. [DOI] [PubMed] [Google Scholar]
  9. Trinick J., Elliott A. Electron microscope studies of thick filaments from vertebrate skeletal muscle. J Mol Biol. 1979 Jun 15;131(1):133–136. doi: 10.1016/0022-2836(79)90304-8. [DOI] [PubMed] [Google Scholar]
  10. Tyler J. M., Anderson J. M., Branton D. Structural comparison of several actin-binding macromolecules. J Cell Biol. 1980 May;85(2):489–495. doi: 10.1083/jcb.85.2.489. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Tyler J. M., Branton D. Rotary shadowing of extended molecules dried from glycerol. J Ultrastruct Res. 1980 May;71(2):95–102. doi: 10.1016/s0022-5320(80)90098-2. [DOI] [PubMed] [Google Scholar]
  12. Wang K., McClure J., Tu A. Titin: major myofibrillar components of striated muscle. Proc Natl Acad Sci U S A. 1979 Aug;76(8):3698–3702. doi: 10.1073/pnas.76.8.3698. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Wang K. Purification of titin and nebulin. Methods Enzymol. 1982;85(Pt B):264–274. doi: 10.1016/0076-6879(82)85025-8. [DOI] [PubMed] [Google Scholar]
  14. Wang K., Williamson C. L. Identification of an N2 line protein of striated muscle. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3254–3258. doi: 10.1073/pnas.77.6.3254. [DOI] [PMC free article] [PubMed] [Google Scholar]

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