Electron microscopy and image analysis of myosin filaments from scallop striated muscle

Vibert, Peter; Craig, Roger

doi:10.1016/s0022-2836(83)80259-9

Cited by 85 publications

(87 citation statements)

References 30 publications

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“…Negative staining EM did not resolve both heads in thick filament 3D reconstructions of other species Similar interpretations were suggested from other arthropods negatively stained thick filament 3D reconstructions such as Limulus (Stewart et al 1981Levine et al 1982) and scorpion Vejovis spinigera (Arachnida) Stewart et al 1985), and from the thick filament 3D reconstruction of the abductor muscle in the scallop Placopecten magellanicus (Mollusca) (Vibert and Craig 1983). The number of helices in the thick filaments was found to be either 3 in vertebrates (frog, Kensler and Stewart 1983;rabbit, Kensler and Stewart 1993), 4 in arthropods (Limulus, (Stewart et al 1981;tarantula, Crowther et al 1985;Padrón et al 1993a;and scorpion, Stewart et al 1985) or 7 in mollusks (scallop, Vibert and Craig 1983;Craig et al 1991).…”

Section: Why Tarantula Muscle?supporting

confidence: 63%

“…The number of helices in the thick filaments was found to be either 3 in vertebrates (frog, Kensler and Stewart 1983;rabbit, Kensler and Stewart 1993), 4 in arthropods (Limulus, (Stewart et al 1981;tarantula, Crowther et al 1985;Padrón et al 1993a;and scorpion, Stewart et al 1985) or 7 in mollusks (scallop, Vibert and Craig 1983;Craig et al 1991). Other EM studies on negatively stained thick filaments have been reported for invertebrates such as the indirect flight muscle (IFM) of the giant water bug Lethocerus indicus (Insecta) (Clarke et al 1986;Morris et al 1991), as well as for skeletal muscle in several vertebrates such as goldfish Carassius auratus (Kensler and Stewart 1989;Eakins et al 2002), frog Rana pipiens Stewart and Kensler 1986), chicken (Kensler and Woodhead 1995) and rabbit (Kensler and Stewart 1993).…”

Section: Why Tarantula Muscle?mentioning

confidence: 99%

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Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function

et al. 2017

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The tarantula skeletal muscle X-ray diffraction pattern suggested that the myosin heads were helically arranged on the thick filaments. Electron microscopy (EM) of negatively stained relaxed tarantula thick filaments revealed four helices of heads allowing a helical 3D reconstruction. Due to its low resolution (5.0 nm), the unambiguous interpretation of densities of both heads was not possible. A resolution increase up to 2.5 nm, achieved by cryo-EM of frozen-hydrated relaxed thick filaments and an iterative helical real space reconstruction, allowed the resolving of both heads. The two heads, Bfree^and Bblocked^, formed an asymmetric structure named the Binteracting-heads motif^(IHM) which explained relaxation by self-inhibition of both heads ATPases. This finding made tarantula an exemplar system for thick filament structure and function studies. Heads were shown to be released and disordered by Ca 2+ -activation through myosin regulatory light chain phosphorylation, leading to EM, small angle X-ray diffraction and scattering, and spectroscopic and biochemical studies of the IHM structure and function. The results from these studies have consequent implications for understanding and explaining myosin super-relaxed state and thick filament activation and regulation. A cooperative phosphorylation mechanism for activation in tarantula skeletal muscle, involving swaying constitutively Ser35 mono-phosphorylated free heads, explains super-relaxation, force potentiation and posttetanic potentiation through Ser45 mono-phosphorylated blocked heads. Based on this mechanism, we propose a swaying-swinging, tilting crossbridge-sliding filament for tarantula muscle contraction.

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Section: Why Tarantula Muscle?supporting

confidence: 63%

Section: Why Tarantula Muscle?mentioning

confidence: 99%

Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function

et al. 2017

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“…The filament has a surface array of myosin cross-bridges with a 14.5 nm axial period, heads (from different helices) coming into register every 10 crowns, and helical "tracks" with a interhelix spacing (helical repeat) of 48 nm (Fig. 6A5) (Vibert and Craig, 1983). The tracks are presumably the strands observed in other thick filaments.…”

Section: 23mentioning

confidence: 99%

“…4A the blue and red helices have pitches of 123.2 and 109.6 nm, respectively. It is also sometimes used (Wray et al, 1975;Vibert and Craig, 1983;Vibert, 1992) as a synonym for 'helical repeat', the distance between sequential helices of the same type. In Fig.…”

Section: 22mentioning

confidence: 99%

“…6A4 (Wray, 1979b). Scallop (Placopecten) striated adductor muscle thick filaments have a diameter of 27 nm and seven fold rotational symmetry (Vibert and Craig, 1983;Craig et al, 1991;Alamo et al, 1991). The filament has a surface array of myosin cross-bridges with a 14.5 nm axial period, heads (from different helices) coming into register every 10 crowns, and helical "tracks" with a interhelix spacing (helical repeat) of 48 nm (Fig.…”

Section: 23mentioning

confidence: 99%

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Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

131

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This is the second in a series of canonical reviews on invertebrate muscle. We cover here thin and thick filament structure, the molecular basis of force generation and its regulation, and two special properties of some invertebrate muscle, catch and asynchronous muscle. Invertebrate thin filaments resemble vertebrate thin filaments, although helix structure and tropomyosin arrangement show small differences. Invertebrate thick filaments, alternatively, are very different from vertebrate striated thick filaments and show great variation within invertebrates. Part of this diversity stems from variation in paramyosin content, which is greatly increased in very large diameter invertebrate thick filaments. Other of it arises from relatively small changes in filament backbone structure, which results in filaments with grossly similar myosin head placements (rotating crowns of heads every 14.5 nm) but large changes in detail (distances between heads in azimuthal registration varying from three to thousands of crowns). The lever arm basis of force generation is common to both vetebrates and invertebrates, and in some invertebrates this process is understood on the near atomic level. Invertebrate actomyosin is both thin (tropomyosin:troponin) and thick (primarily via direct Ca ++ binding to myosin) filament regulated, and most invertebrate muscles are dually regulated. These mechanisms are well understood on the molecular level, but the behavioral utility of dual regulation is less so. The phosphorylation state of the thick filament associated giant protein, twitchin, has been recently shown to be the molecular basis of catch. The molecular basis of the stretch activation underlying asynchronous muscle activity, however, remains unresolved.

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Protein machines and self assembly in muscle organization

Barral

Epstein

1999

Bioessays

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The remarkable order of striated muscle is the result of a complex series of protein interactions at different levels of organization. Within muscle, the thick filament and its major protein myosin are classical examples of functioning protein machines. Our understanding of the structure and assembly of thick filaments and their organization into the regular arrays of the A‐band has recently been enhanced by the application of biochemical, genetic, and structural approaches. Detailed studies of the thick filament backbone have shown that the myosins are organized into a tubular structure. Additional protein machines and specific myosin rod sequences have been identified that play significant roles in thick filament structure, assembly, and organization. These include intrinsic filament components, cross‐linking molecules of the M‐band and constituents of the membrane‐cytoskeleton system. Muscle organization is directed by the multistep actions of protein machines that take advantage of well‐established self‐assembly relationships. BioEssays 21:813–823, 1999. © 1999 John Wiley & Sons, Inc.

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Electron microscopy and image analysis of myosin filaments from scallop striated muscle

Cited by 85 publications

References 30 publications

Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function

Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Protein machines and self assembly in muscle organization

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