Identification of sequence changes in myosin II that adjust muscle contraction velocity

Autor: Anthony J. Baines, Jonathan Walklate, Marta Farré, Michael A. Geeves, Carlos Vera, Mark N. Wass, Daniel P. Mulvihill, Jake E McGreig, Chloe A. Johnson, Martin S. Ridout, Leslie A. Leinwand, Sarah T. Jeanfavre
Přispěvatelé: Johnson, Chloe A [0000-0003-0856-5041], Vera, Carlos D [0000-0003-1207-4878], Farré, Marta [0000-0001-9170-5767], Mulvihill, Daniel P [0000-0003-2502-5274], Wass, Mark N [0000-0001-5428-6479], Geeves, Michael A [0000-0002-9364-8898], Apollo - University of Cambridge Repository
Rok vydání: 2021
Předmět:
Contraction (grammar)
Muscle Physiology
Physiology
Protein Sequencing
Q1
Biochemistry
Contractile Proteins
Adenosine Triphosphate
CrossBridge
Myosin
Medicine and Health Sciences
Protein Isoforms
Biology (General)
Musculoskeletal System
Conserved Sequence
Phylogeny
Data Management
Mammals
0303 health sciences
General Neuroscience
Muscles
030302 biochemistry & molecular biology
Cardiac muscle
Eukaryota
Phylogenetic Analysis
Adaptation
Physiological
Cell biology
Phylogenetics
Adenosine Diphosphate
medicine.anatomical_structure
Vertebrates
Amino Acid Analysis
medicine.symptom
Anatomy
General Agricultural and Biological Sciences
Muscle contraction
Research Article
Muscle Contraction
Gene isoform
Computer and Information Sciences
QH301-705.5
Motor Proteins
Actin Motors
Motility
macromolecular substances
Biology
Myosins
Research and Analysis Methods
General Biochemistry
Genetics and Molecular Biology
Cell Line
03 medical and health sciences
Protein Domains
Molecular Motors
medicine
Animals
Humans
Evolutionary Systematics
Amino Acid Sequence
Molecular Biology Techniques
Sequencing Techniques
Molecular Biology
030304 developmental biology
Sequence (medicine)
Taxonomy
Cardiac Muscles
Myosin Type II
Evolutionary Biology
Molecular Biology Assays and Analysis Techniques
General Immunology and Microbiology
Body Weight
Organisms
Biology and Life Sciences
Proteins
Cell Biology
Rats
Cytoskeletal Proteins
Amniotes
Zoology
Zdroj: PLoS Biology
PLOS Biology
PLoS Biology, Vol 19, Iss 6, p e3001248 (2021)
PLoS Biology, Vol 19, Iss 6 (2021)
ISSN: 1544-9173
Popis: The speed of muscle contraction is related to body size; muscles in larger species contract at slower rates. Since contraction speed is a property of the myosin isoform expressed in a muscle, we investigated how sequence changes in a range of muscle myosin II isoforms enable this slower rate of muscle contraction. We considered 798 sequences from 13 mammalian myosin II isoforms to identify any adaptation to increasing body mass. We identified a correlation between body mass and sequence divergence for the motor domain of the 4 major adult myosin II isoforms (β/Type I, IIa, IIb, and IIx), suggesting that these isoforms have adapted to increasing body mass. In contrast, the non-muscle and developmental isoforms show no correlation of sequence divergence with body mass. Analysis of the motor domain sequence of β-myosin (predominant myosin in Type I/slow and cardiac muscle) from 67 mammals from 2 distinct clades identifies 16 sites, out of 800, associated with body mass (padj < 0.05) but not with the clade (padj > 0.05). Both clades change the same small set of amino acids, in the same order from small to large mammals, suggesting a limited number of ways in which contraction velocity can be successfully manipulated. To test this relationship, the 9 sites that differ between human and rat were mutated in the human β-myosin to match the rat sequence. Biochemical analysis revealed that the rat–human β-myosin chimera functioned like the native rat myosin with a 2-fold increase in both motility and in the rate of ADP release from the actin–myosin crossbridge (the step that limits contraction velocity). Thus, these sequence changes indicate adaptation of β-myosin as species mass increased to enable a reduced contraction velocity and heart rate.
Heart and skeletal muscles of larger mammals contract more slowly than smaller ones. This study identifies amino acid changes in myosin isoforms that correlate with species size; mutating the residues in human β-myosin to match the rat sequence at these positions increased its in vitro velocity to that of the rat protein.
Databáze: OpenAIRE
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