The native subunit pattern of tropomyosin

Strasburg, Gale M.; Greaser, Marion L.

doi:10.1016/0014-5793(76)80802-2

Cited by 22 publications

(13 citation statements)

References 14 publications

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“…If Tm- is the exclusive or predominant isoform in some jaw-closing muscles, then it presumably is present, in large part, as  dimers in the same muscles. This would be unusual but not unprecedented, as others (Holtzer et al, 1992) have reported that Tm- dimers are present in mammalian skeletal muscle, but at relatively low levels (≤10% of total Tm), as well as in avian smooth muscle (Strasburg and Greaser, 1976). The apparent exclusive expression of Tm- in some muscles, reported here, is a novel finding.…”

Section: Discussionsupporting

confidence: 74%

Patterns of tropomyosin and troponin-T isoform expression in jaw-closing muscles of mammals and reptiles that express masticatory myosin

Bicer

Patel

Williams

et al. 2011

Journal of Experimental Biology

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SUMMARYWe recently reported that masticatory ('superfast') myosin is expressed in jaw-closing muscles of some rodent species. Most mammalian limb muscle fibers express tropomyosin- (Tm-), along with fast-type or slow-type tropomyosin-a (Tm-a), but jawclosing muscle fibers in members of Carnivora express a unique isoform of Tm [Tm-masticatory (Tm-M)] and little or no Tm-. The goal of this study was to determine patterns of Tm and troponin-T (TnT) isoform expression in the jaw-closing muscles of rodents and other vertebrate species that express masticatory myosin, and compare the results to those from members of Carnivora. Comparisons of electrophoretic mobility, immunoblotting and mass spectrometry were used to probe the Tm and fast-type TnT isoform composition of jaw-closing and limb muscles of six species of Carnivora, eight species of Rodentia, five species of Marsupialia, big brown bat, long-tailed macaque and six species of Reptilia. Extensive heterogeneity exists in Tm and TnT isoform expression in jaw-closing muscles between phylogenetic groups, but there are fairly consistent patterns within each group. We propose that the differences in Tm and TnT isoform expression patterns between phylogenetic groups, which share the expression of masticatory myosin, may impart fundamental differences in thin-filament-mediated muscle activation to accommodate markedly different feeding styles that may require high force generation in some species (e.g. many members of Carnivora) and high speed in others (e.g. Rodentia).

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Section: Discussionsupporting

confidence: 74%

Patterns of tropomyosin and troponin-T isoform expression in jaw-closing muscles of mammals and reptiles that express masticatory myosin

Bicer

Patel

Williams

et al. 2011

Journal of Experimental Biology

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“…In some extant studies of RSTm, no 00 molecules were detected by hydroxyapatite chromatography or Laemmli sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE) (Eisenberg & Kielley, 1974;Strasburg & Greaser, 1976). This result has won wide acceptance.…”

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confidence: 99%

“…In rabbit skeletal tropomyosin (RSTm), a and 0 chains are present in a 3-4:l ratio, and 00 and ap, in an -3.2 ratio, are the predominant molecular species (Eisenberg & Kielley, 1974;Lehrer, 1975;Strasburg & Greaser, 1976).…”

mentioning

confidence: 99%

ββ homodimers exist in native rabbit skeletal muscle tropomyosin and increase after denaturation–renaturation

et al. 1992

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Native tropomyosin from rabbit skeletal muscle (RSTm) consists mainly of aa and (YO coiled coils (a/@ = 3-4/1).In some extant studies, no (30 molecules have been found. In this study, RSTm from several different preparations was disulfide cross-linked, both preparation and cross-linking being done under nondenaturing conditions. The cross-linked product was assayed for the presence of molecules cross-linked at both C36 and C190 (p=p). In such cross-linked RSTm, 3-8070 /3=p is detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis, C4 reversed-phase high-performance liquid chromatography, and a free-solution capillary electrophoresis experiment. This percentage becomes -4-10070 pp when corrected for incomplete double cross-linking and is independent of protein concentration (0.1-10.0 mg/mL), indicating that the observed p/3 species are not artifacts due to intermolecular cross-linking. Upon denaturation and subsequent renaturation either by heating to 55 "C or by incubating at 45 "C followed by quenching to room temperature, or by guanidine hydrochloride exposure followed by phased renaturation by dialysis, the fraction of increases, indicating that the reassociation favors homodimer formation somewhat over random association. This result differs from the random association observed when the sulfhydryl on one of the chains is carboxyamidomethylated (Holtzer, M.E., Breiner, T., & Holtzer, A . , 1984, Biopolymers 23, 181 1-1833), and from the overwhelming heterodimer preferences reported for tropomyosins from other organisms

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“…The faster migrating component within any one system has been conventionally termed cu-tropomyosin and the slower migrating one, ,8-tropomyosin [3]. In the case of gizzard tropomyosin therefore, the components migrating with an apparent molecular mass of 43 and 33 kDa (the 43K and the 33K components) have been considered as ,&tropomyosin and cu-tropomyosin respectively, from smooth muscle [12].…”

Section: Tropomyosi~ Fractionationmentioning

confidence: 99%

Classification of tropomyosin components into an α‐like or a β‐like family by partial peptide mapping

Kardami

Fiszman

1983

FEBS Letters

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Tropomyosins can be classified as belonging to an a-like or a &like family depending on the absence or presence, respectively, in their protease-V8 digestion pattern of two peptides with an apparent molecular mass of 21 kDa. Chicken cardiac tropomyosin and the 43 kDa component from gizzard tropomyosin are accordingly classified as a-like tropomyosins, while the 33 kDa gizzard tropomyosin component is aBlike tropomyosin. The 21 kDa peptides have an overall charge which is more positive than that of the intact tropomyosin or any other tropomyosin peptide and probably contain the -NH2 half of the molecule. Tropomyosin classificationPartiaf peptide mapping p-Tropomyosin 'dgference' peptide

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The native subunit pattern of tropomyosin

Cited by 22 publications

References 14 publications

Patterns of tropomyosin and troponin-T isoform expression in jaw-closing muscles of mammals and reptiles that express masticatory myosin

Patterns of tropomyosin and troponin-T isoform expression in jaw-closing muscles of mammals and reptiles that express masticatory myosin

ββ homodimers exist in native rabbit skeletal muscle tropomyosin and increase after denaturation–renaturation

Classification of tropomyosin components into an α‐like or a β‐like family by partial peptide mapping

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