Molecular Evolution of the Myosin Family: Relationships Derived from Comparisons of Amino Acid Sequences

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, demonstra...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1993-01, Vol.90 (2), p.659-663
Main Authors: Goodson, Holly V., Spudich, James A.
Format: Article
Language:English
Subjects:
Amino acids
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Biological Evolution
Classification
Contractile proteins
Drosophila
Evolution
Fundamental and applied biological sciences. Psychology
Holoproteins
Multigene Family
Muscles
Muscles - chemistry
Myosins - classification
Myosins - genetics
Parsimony
Phylogenetics
Protein Conformation
Protein isoforms
Proteins
Sequence Alignment - methods
Sequence Homology, Amino Acid
Smooth muscle
Software
Striated muscle
Yeasts
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Summary: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 non-muscle 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.90.2.659