Amino acid sequences of the two major isoforms of troponin C from crayfish

Kobayashi, Tomoyoshi; Takagi, Takashi; Konishi, Kazuhiko; Wnuk, W

doi:10.1016/s0021-9258(19)84704-x

Cited by 55 publications

(17 citation statements)

References 32 publications

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“…In the process of making an antibody to troponin C we noted that bacterially expressed wild-type nematode troponin C appeared to have intact calcium-binding capability. We were able to detect mobility shifts of troponin C (Fyrberg et al, 1994), crayfish type (Kobayashi et al, 1989), rabbits, cardiac (Wilkinson, 1980) and skeletal (Zot et al, 1987). produced in bacteria in the presence or absence of calcium on SDS-PAGE followed by Western blot analysis (Fig.…”

Section: A Mutation In Troponin C Affects Calcium and Troponin I Bindingmentioning

confidence: 98%

“…CeTNC-1 is most similar to the other invertebrate proteins, and has overall sequence identities of 48.2, 44.7, and 40.4% to C . elegans CeTNC-2, Drosophila TNC73F (Fyrberg et al, 1994), and the crayfish troponin C alpha isoform (Kobayashi et al, 1989), respectively. Sequence identifies to the rabbit cardiac and skeletal isoforms are 33.9 and 28.6%, respectively.…”

Section: Identification and Structure Of A Troponin C Gene Of C Elegansmentioning

confidence: 99%

“…The Drosophila Dm73F and the crayfish alpha isoforms have several inappropriately charged residues at the ion coordination sites within EF-hand domains I and III (Fig. 3), suggesting that these domains can not bind calcium ions (Kobayashi et al, 1989;Collins et al, 1991). Site I of the rabbit cardiac muscle protein may also be nonfunctional.…”

Section: Identification and Structure Of A Troponin C Gene Of C Elegansmentioning

confidence: 99%

“…This protein binds four calcium ions and forms a complex with both troponin I and troponin T (Ebashi and Endo, 1968;Ohtsuki et al, 1986;Grabarek et al, 1992). Troponin C was first isolated and sequenced from skeletal and cardiac muscles of vertebrates (Collins et al, 1977;Wilkinson, 1980;Gahlmann and Kedes, 1990), but has also been isolated from invertebrates including crayfish (Kobayashi et al, 1989), scallops (Ojima et al, 1994), nematodes (Kimura et al, 1987), and insects (Bullard et al, 1988). Much is known about the structure and biochemical details of how this protein functions (Herzberg and James, 1988;Reinach and Karlsson, 1988;Parmacek and Leiden, 1989;Fujimori et al, 1990;Parmacek et al, 1990Parmacek et al, , 1992Schreier et al, 1990;Smith et al, 1994), including its calcium-binding properties (Putkey et al, 1989) and sites for interaction with troponin I (Tripet et al, 1997;Vassylyev et al, 1998), but little is known about the consequence of altering some of these functional properties within a developmental con-text.…”

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confidence: 99%

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Genomic Organization, Expression, and Analysis of the Troponin C Gene pat-10 of Caenorhabditis elegans

Terami¹

1999

The Journal of Cell Biology

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Abstract.We have cloned and characterized the troponin C gene, pat-10 of the nematode Caenorhabditis elegans . At the amino acid level nematode troponin C is most similar to troponin C of Drosophila (45% identity) and cardiac troponin C of vertebrates. Expression studies demonstrate that this troponin is expressed in body wall muscle throughout the life of the animal. Later, vulval muscles and anal muscles also express this troponin C isoform. The structural gene for this troponin is pat-10 and mutations in this gene lead to animals that arrest as twofold paralyzed embryos late in development. We have sequenced two of the mutations in pat-10 and both had identical two mutations in the gene; one changes D64 to N and the other changes W153 to a termination site. The missense alteration affects a calcium-binding site and eliminates calcium binding, whereas the second mutation eliminates binding to troponin I. These combined biochemical and in vivo studies of mutant animals demonstrate that this troponin is essential for proper muscle function during development.

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Section: A Mutation In Troponin C Affects Calcium and Troponin I Bindingmentioning

confidence: 98%

Section: Identification and Structure Of A Troponin C Gene Of C Elegansmentioning

confidence: 99%

Section: Identification and Structure Of A Troponin C Gene Of C Elegansmentioning

confidence: 99%

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confidence: 99%

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Genomic Organization, Expression, and Analysis of the Troponin C Gene pat-10 of Caenorhabditis elegans

Terami¹

1999

The Journal of Cell Biology

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“…Fibre-type-specific isoforms of myosin heavy and light chains, tropomyosin, paramyosin and troponin-I, -T and -C are expressed in lobster and crayfish muscles (Mykles, 1985a,b;Kobayashi et al, 1989;Li and Mykles, 1990;Miyazaki et al, 1990Miyazaki et al, , 1992Miyazaki et al, , 1993Nishita and Ojima, 1990;Garone et al, 1991;Miegel et al, 1992;Cotton and Mykles, 1993;Neil et al, 1993;Galler and Neil, 1994;Sakurai et al, 1996;Ishimoda-Takagi et al, 1997;Cooper et al, 1998;Mykles et al, 1998;Holmes et al, 1999;LaFramboise et al, 1999;Sohn et al, 2000). However, for an isoform to serve as a suitable diagnostic marker, it must (i) be exclusively expressed in a specific fibre type in various decapod crustacean species and (ii) be easily distinguished in SDS-polyacrylamide gels.…”

Section: Introductionmentioning

confidence: 99%

Myofibrillar protein isoform expression is correlated with synaptic efficacy in slow fibres of the claw and leg opener muscles of crayfish and lobster

Mykles

Medler

Koenders

et al. 2002

Journal of Experimental Biology

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SUMMARY In the crayfish and lobster opener neuromuscular preparations of the walking legs and claws, there are regional differences in synaptic transmission even though the entire muscle is innervated by a single excitatory tonic motor neuron. The innervation of the proximal fibres produced larger excitatory postsynaptic potentials (EPSPs) than those of the central fibres. The amplitudes of the EPSPs in the distal fibres were intermediate between those of the proximal and central regions. These differences in EPSP amplitudes were correlated with differences in short-term facilitation between the three regions. When given a 10- or 20-pulse train of stimuli, the proximal fibres showed greater short-term facilitation initially, often followed by a maximization of short-term facilitation towards the end of a train. In contrast, the central fibres showed a linear increase in short-term facilitation throughout a stimulus train. The distal fibres showed intermediate short-term facilitation compared with the other two regions. Analysis of myofibrillar isoforms showed that levels of troponin-T1 (TnT1), a 55 kDa isoform expressed in slow-tonic (S2) fibres, were correlated with synaptic properties. Proximal fibres had the highest levels of TnT1, with lower levels in distal fibres; central fibres lacked TnT1, which is characteristic of slow-twitch (S1) fibres. In addition, differences in troponin-I isoforms correlated with TnT1 levels between the proximal, central and distal regions. The correlation between slow fibre phenotype and strength of innervation suggests a relationship between synaptic structure and expression of troponin isoforms.

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Immunocytochemical electron microscopic study and western blot analysis of troponin in striated muscle of the fruit flyDrosophila melanogaster and in several muscle cell types of the earthwormEisenia foetida

et al. 1996

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Background There is little information about troponin in invertebrate muscles, and no previous references to this protein in annelid muscles have been found. The aim of this paper was to study the presence and distribution of troponin in different muscle cell types from the earthworm Eisenia foetida (the muscular body wall, and the inner and outer muscular layer of the pseudoheart). These results were compared with those obtained in the transversely striated muscle of Drosophila melanogaster and in skeletal and smooth muscles of the mouse. Methods Immunocytochemical electron microscopic study and Western blot analysis using anti‐TnT antibodies were employed in this study. Results Troponin immunoreaction was detected in the mouse skeletal muscle, the fly flight muscle, and earthworm obliquely striated muscles (body wall musculature and inner muscular layer of the pseudoheart). Immunolabeling for TnT in all these muscle cells appeared in moderate amounts at any point along the sarcomere length, except for the central zone of the A band (H band). This suggests that troponin molecules were located along the thin filaments. The density of immunogold particles was similar in the three muscles, and thus the amount of troponin in each muscle type was proportional to the number and length of actin filaments in each. Troponin was found in neither the mouse smooth muscle nor the outer muscular layer of the earthworm pseudoheart. The latter muscle showed an ultrastructural pattern that was intermediate between obliquely striated and smooth muscle. The estimated molecular weight for TnT in the earthworm was 55 kDa; this is higher than the weight of this protein in the mouse skeletal muscle (40 kDa) but similar to that of the D. melanogaster muscle (52 kDa). Conclusions Troponin is present in both types of striated muscle (transversely striated and obliquely striated) of the earthworm with a distribution that is very similar to that observed in the mammalian striated muscle. As in vertebrates, troponin is absent in the smooth muscle of the earthworm. Discrepancies in the classification of some invertebrate muscles are common in the literature, and the use of distinctive markers, such as troponin, may improve our understanding of the nature and properties of many invertebrate muscles showing an ultrastructural pattern that does not resemble any of the classic muscle types. © 1996 Wiley‐Liss, Inc.

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Amino acid sequences of the two major isoforms of troponin C from crayfish

Cited by 55 publications

References 32 publications

Genomic Organization, Expression, and Analysis of the Troponin C Gene pat-10 of Caenorhabditis elegans

Genomic Organization, Expression, and Analysis of the Troponin C Gene pat-10 of Caenorhabditis elegans

Myofibrillar protein isoform expression is correlated with synaptic efficacy in slow fibres of the claw and leg opener muscles of crayfish and lobster

Immunocytochemical electron microscopic study and western blot analysis of troponin in striated muscle of the fruit flyDrosophila melanogaster and in several muscle cell types of the earthwormEisenia foetida

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