Sea Lily Muscle Lacks a Troponin-Regulatory System, While it Contains Paramyosin

Obinata, Takashi; Amemiya, Shonan; Takai, Ryosuke; Ichikawa, Muneyoshi; Toyoshima, Yoko Y.; Sato, Naruki

doi:10.2108/zsj.31.122

Cited by 7 publications

(5 citation statements)

References 38 publications

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“…By contrast, within the Deuterostomia, our homology search in the genome of the sea urchin Strongylocentrotus purpuratus [Sea Urchin Genome Sequencing Consortium, 2006] failed to detect a troponin component. This is consistent with earlier biochemical studies showing the absence of a troponin-like protein in muscles of sea urchin [Obinata et al, 1974], sea cucumber [Lehman and Szent-Gyorgyi, 1975], and sea lily [Obinata et al, 2014], suggesting strongly that the phylum Echinodermata lacks troponin ( Fig. 1).…”

Section: Resultssupporting

confidence: 93%

Molecular evolution of troponin I and a role of its N‐terminal extension in nematode locomotion

et al. 2016

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Summary The troponin complex, composed of troponin T (TnT), troponin I (TnI), and troponin C (TnC), is the major calcium-dependent regulator of muscle contraction, which is present widely in both vertebrates and invertebrates. Little is known about evolutionary aspects of troponin in the animal kingdom. Using a combination of data mining and functional analysis of TnI, we report evidence that an N-terminal extension of TnI is present in most of bilaterian animals as a functionally important domain. Troponin components have been reported in species in most of representative bilaterian phyla. Comparison of TnI sequences shows that the core domains are conserved in all examined TnIs, and that N- and C-terminal extensions are variable among isoforms and species. In particular, N-terminal extensions are present in all protostome TnIs and chordate cardiac TnIs but lost in a subset of chordate TnIs including vertebrate skeletal-muscle isoforms. Transgenic rescue experiments in C. elegans striated muscle show that the N-terminal extension of TnI (UNC-27) is required for coordinated worm locomotion but not in sarcomere assembly and single muscle-contractility kinetics. These results suggest that N-terminal extensions of TnIs are retained from a TnI ancestor as a functional domain.

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Section: Resultssupporting

confidence: 93%

Molecular evolution of troponin I and a role of its N‐terminal extension in nematode locomotion

et al. 2016

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show abstract

“…By contrast, within the Deuterostomia, our homology search in the genome of the sea urchin Strongylocentrotus purpuratus (Sea Urchin Genome Sequencing Consortium et al 2006) failed to detect a troponin component. This is consistent with earlier biochemical studies showing the absence of a troponin-like protein in muscles of sea urchin (Obinata et al 1974), sea cucumber (Lehman and Szent-Gyorgyi 1975), and sea lily (Obinata et al 2014), suggesting strongly that the phylum Echinodermata lacks troponin (Fig. 1).…”

Section: Troponin Evolved Early In the Bilateriasupporting

confidence: 92%

Molecular evolution of troponin I and a role of its N‐terminal extension in nematode locomotion

et al. 2016

View full text Add to dashboard Cite

The troponin complex, composed of troponin T (TnT), troponin I (TnI), and troponin C (TnC), is the major calcium-dependent regulator of muscle contraction, which is present widely in both vertebrates and invertebrates. Little is known about evolutionary aspects of troponin in the animal kingdom. Using a combination of data mining and functional analysis of TnI, we report evidence that an N-terminal extension of TnI is present in most of bilaterian animals as a functionally important domain. Troponin components have been reported in species in most of representative bilaterian phyla. Comparison of TnI sequences shows that the core domains are conserved in all examined TnIs, and that N-and C-terminal extensions are variable among isoforms and species. In particular, N-terminal extensions are present in all protostome TnIs and chordate cardiac TnIs but lost in a subset of chordate TnIs including vertebrate skeletal-muscle isoforms. Transgenic rescue experiments in C. elegans striated muscle show that the N-terminal extension of TnI (UNC-27) is required for coordinated worm locomotion but not in sarcomere assembly and single musclecontractility kinetics. These results suggest that N-terminal extensions of TnIs are retained from a TnI ancestor as a functional domain.

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“…By covering the myosin-binding sites of actin molecules, tropomyosin prevents muscle contraction. Biochemical analyses suggest the existence of tropomyosin in muscles of a sea lily (Echinodermata) ( Obinata et al. 2014 ) and an acorn worm (Hemichordata) ( Sonobe et al.…”

Section: Resultsmentioning

confidence: 99%

Deuterostome Genomics: Lineage-Specific Protein Expansions That Enabled Chordate Muscle Evolution

Inoue

Satoh

2018

Molecular Biology and Evolution

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Fish-like larvae were foundational to the chordate body plan, given the basal placement of free-living lancelets. That body plan probably made it possible for chordate ancestors to swim by beating a tail formed of notochord and bilateral paraxial muscles. In order to investigate the molecular genetic basis of the origin and evolution of paraxial muscle, we deduced the evolutionary histories of 16 contractile protein genes from paraxial muscle, based on genomic data from all five deuterostome lineages, using a newly developed orthology identification pipeline and a species tree. As a result, we found that more than twice as many orthologs of paraxial muscle genes are present in chordates, as in nonchordate deuterostomes (ambulacrarians). Orthologs of paraxial-type actin and troponin C genes are absent in ambulacrarians and most paraxial muscle protein isoforms diversified via gene duplications that occurred in each chordate lineage. Analyses of genes with known expression sites indicated that some isoforms were reutilized in specific muscles of nonvertebrate chordates via gene duplications. As orthologs of most paraxial muscle genes were present in ambulacrarians, in addition to expression patterns of related genes and functions of the two protein isoforms, regulatory mechanisms of muscle genes should also be considered in future studies of the origin of paraxial muscle.

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Sea Lily Muscle Lacks a Troponin-Regulatory System, While it Contains Paramyosin

Cited by 7 publications

References 38 publications

Molecular evolution of troponin I and a role of its N‐terminal extension in nematode locomotion

Molecular evolution of troponin I and a role of its N‐terminal extension in nematode locomotion

Molecular evolution of troponin I and a role of its N‐terminal extension in nematode locomotion

Deuterostome Genomics: Lineage-Specific Protein Expansions That Enabled Chordate Muscle Evolution

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