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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
. 1993 Jan 15;90(2):659–663. doi: 10.1073/pnas.90.2.659

Molecular evolution of the myosin family: relationships derived from comparisons of amino acid sequences.

H V Goodson 1, J A Spudich 1
PMCID: PMC45723  PMID: 8421702

Abstract

To examine the evolutionary relationships between members of the myosin family, we have used two different phylogenetic methods, distance matrix and maximum parsimony, to analyze all available myosin head sequences. We find that there are at least three equally divergent classes of myosin, demonstrating that the current classification of myosin into only two classes needs to be reexamined. In the myosin II class, smooth muscle myosin is more closely related to nonmuscle myosin than to striated muscle myosin, implying that smooth muscle and skeletal muscle myosins were independently derived from nonmuscle myosin and suggesting that similarities between these types of muscle are the result of convergent evolution. The grouping of head sequences produced by phylogenetic analysis is consistent with classifications based on enzymology and structural localization and is generally consistent with grouping based on common tail structure elements. This result demonstrates that specific head sequences are tightly coupled to specific tail sequences throughout evolution and challenges the idea that myosin heads are freely interchangeable units whose unique function is determined only by the tail structure to which it is attached.

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Selected References

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  1. Cheney R. E., Mooseker M. S. Unconventional myosins. Curr Opin Cell Biol. 1992 Feb;4(1):27–35. doi: 10.1016/0955-0674(92)90055-h. [DOI] [PubMed] [Google Scholar]
  2. Collins J. H. Myosin light chains and troponin C: structural and evolutionary relationships revealed by amino acid sequence comparisons. J Muscle Res Cell Motil. 1991 Feb;12(1):3–25. doi: 10.1007/BF01781170. [DOI] [PubMed] [Google Scholar]
  3. Emerson C. P., Jr, Bernstein S. I. Molecular genetics of myosin. Annu Rev Biochem. 1987;56:695–726. doi: 10.1146/annurev.bi.56.070187.003403. [DOI] [PubMed] [Google Scholar]
  4. Felsenstein J. Phylogenies from molecular sequences: inference and reliability. Annu Rev Genet. 1988;22:521–565. doi: 10.1146/annurev.ge.22.120188.002513. [DOI] [PubMed] [Google Scholar]
  5. Feng D. F., Doolittle R. F. Progressive alignment and phylogenetic tree construction of protein sequences. Methods Enzymol. 1990;183:375–387. doi: 10.1016/0076-6879(90)83025-5. [DOI] [PubMed] [Google Scholar]
  6. Fitch W. M., Margoliash E. Construction of phylogenetic trees. Science. 1967 Jan 20;155(3760):279–284. doi: 10.1126/science.155.3760.279. [DOI] [PubMed] [Google Scholar]
  7. Fukui Y., Lynch T. J., Brzeska H., Korn E. D. Myosin I is located at the leading edges of locomoting Dictyostelium amoebae. Nature. 1989 Sep 28;341(6240):328–331. doi: 10.1038/341328a0. [DOI] [PubMed] [Google Scholar]
  8. George E. L., Ober M. B., Emerson C. P., Jr Functional domains of the Drosophila melanogaster muscle myosin heavy-chain gene are encoded by alternatively spliced exons. Mol Cell Biol. 1989 Jul;9(7):2957–2974. doi: 10.1128/mcb.9.7.2957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Higgins D. G., Bleasby A. J., Fuchs R. CLUSTAL V: improved software for multiple sequence alignment. Comput Appl Biosci. 1992 Apr;8(2):189–191. doi: 10.1093/bioinformatics/8.2.189. [DOI] [PubMed] [Google Scholar]
  10. Katsuragawa Y., Yanagisawa M., Inoue A., Masaki T. Two distinct nonmuscle myosin-heavy-chain mRNAs are differentially expressed in various chicken tissues. Identification of a novel gene family of vertebrate non-sarcomeric myosin heavy chains. Eur J Biochem. 1989 Oct 1;184(3):611–616. doi: 10.1111/j.1432-1033.1989.tb15057.x. [DOI] [PubMed] [Google Scholar]
  11. Klotz L. C., Blanken R. L. A practical method for calculating evolutionary trees from sequence data. J Theor Biol. 1981 Jul 21;91(2):261–272. doi: 10.1016/0022-5193(81)90233-2. [DOI] [PubMed] [Google Scholar]
  12. Korn E. D., Hammer J. A., 3rd Myosin I. Curr Opin Cell Biol. 1990 Feb;2(1):57–61. doi: 10.1016/s0955-0674(05)80031-6. [DOI] [PubMed] [Google Scholar]
  13. Matsuoka R., Beisel K. W., Furutani M., Arai S., Takao A. Complete sequence of human cardiac alpha-myosin heavy chain gene and amino acid comparison to other myosins based on structural and functional differences. Am J Med Genet. 1991 Dec 15;41(4):537–547. doi: 10.1002/ajmg.1320410435. [DOI] [PubMed] [Google Scholar]
  14. Moncrief N. D., Kretsinger R. H., Goodman M. Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences. J Mol Evol. 1990 Jun;30(6):522–562. doi: 10.1007/BF02101108. [DOI] [PubMed] [Google Scholar]
  15. Moore L. A., Tidyman W. E., Arrizubieta M. J., Bandman E. Gene conversions within the skeletal myosin multigene family. J Mol Biol. 1992 Jan 5;223(1):383–387. doi: 10.1016/0022-2836(92)90741-2. [DOI] [PubMed] [Google Scholar]
  16. Pollard T. D., Doberstein S. K., Zot H. G. Myosin-I. Annu Rev Physiol. 1991;53:653–681. doi: 10.1146/annurev.ph.53.030191.003253. [DOI] [PubMed] [Google Scholar]
  17. Stedman H. H., Eller M., Jullian E. H., Fertels S. H., Sarkar S., Sylvester J. E., Kelly A. M., Rubinstein N. A. The human embryonic myosin heavy chain. Complete primary structure reveals evolutionary relationships with other developmental isoforms. J Biol Chem. 1990 Feb 25;265(6):3568–3576. [PubMed] [Google Scholar]
  18. Stewart A. F., Camoretti-Mercado B., Perlman D., Gupta M., Jakovcic S., Zak R. Structural and phylogenetic analysis of the chicken ventricular myosin heavy chain rod. J Mol Evol. 1991 Oct;33(4):357–366. doi: 10.1007/BF02102866. [DOI] [PubMed] [Google Scholar]
  19. Warrick H. M., Spudich J. A. Myosin structure and function in cell motility. Annu Rev Cell Biol. 1987;3:379–421. doi: 10.1146/annurev.cb.03.110187.002115. [DOI] [PubMed] [Google Scholar]

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