Paramyosin in invertebrate muscles. II. Content in relation to structure and function.

Levine, Rhea J. C.; Elfvin, Myra; Dewey, Maynard M.; Walcott, Benjamin

doi:10.1083/jcb.71.1.273

Cited by 109 publications

(67 citation statements)

References 26 publications

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“…As noted above, another way to increase the amount of force a sarcomere can produce is to increase thick filament length, and thick filament length does increase with paramyosin content (Levine et al, 1976). Both of these force-increasing effects would increase stress on the thick and thin filaments.…”

Section: 21mentioning

confidence: 97%

“…For instance, although some invertebrate thick filaments have 'typical' 20-30 nm diameters, others, particularly (but not only) molluscan smooth muscles, have very large (60-160 nm) thick filaments (Limulus telson (Levine et al, 1973), echinodermata (Baccetti and Rosati, 1968), amphioxus notochord (Flood et al, 1969;Yongshui and Zuxun, 1979), annelid (Lanzavecchia and de Eguileor, 1976;Camatini et al, 1976;Lanzavecchia, 1977), Nematomorpha (Swanson, 1971b;Lanzavecchia, 1977;Lanzavecchia et al, 1977), mollusc (Jakus et al, 1944;Philpott et al, 1960;Hanson and Lowy, 1961;Lowy and Hanson, 1962;Elliott, 1964a;Kalamkarova and Kriukova, 1966;Kryukova, 1968;Szent-Györgyi et al, 1971;Levine et al, 1976)). Thick filament structure varies even in single muscles-clam adductor (smooth) muscle contains both short (7.5 μm) thin (26.5 nm diameter) and long (13 μm) thick (42 nm diameter) thick filaments (Matsuno et al, 1993).…”

Section: Thick Filamentmentioning

confidence: 99%

“…A protein that plays a central role in determining thick filament diameter is paramyosin. Paramyosin is present not only in large diameter thick filaments, but also in small diameter thick filaments in a large number of species including scallop striated adductor (Levine et al, 1976;Winkelman, 1976), insect flight and body (Bullard et al, 1973b;Levine et al, 1976;Winkelman, 1976;Reedy et al, 1981;Beinbrech et al, 1985;Hinkel-Aust et al, 1990), Limulus (Levine et al, 1976(Levine et al, , 1983Iwatsuki, 1981;Gaylinn and Dewey, 1986), tarantula (Levine et al, 1983), crustacea (Levine et al, 1976;Winkelman, 1976), and nematode Winkelman, 1976) muscle, with paramyosin:myosin mass ratios between 0.03 and 0.7 (Levine et al, 1976;Winkelman, 1976;Iwatsuki, 1981;Gaylinn and Dewey, 1986). However, paramyosin content is greatly increased in large diameter thick filaments (paramyosin:myosin ratios as great as 10:1, and paramyosin comprising up to half the muscle's structural proteins, and 80% of thick filament weight) Rüegg, 1961b;Szent-Györgyi et al, 1971;Elliott, 1974;Levine et al, 1976;Winkelman, 1976;Margulis et al, 1979;Iwatsuki, 1981).…”

Section: 21mentioning

confidence: 99%

“…Nonetheless, paramyosin content is clearly greatly increased in the thick filaments of some muscles, many of which can generate great force Levine et al, 1976;Mukou et al, 2004). These two properties can be interrelated as follows.…”

Section: 21mentioning

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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Section: 21mentioning

confidence: 97%

Section: Thick Filamentmentioning

confidence: 99%

Section: 21mentioning

confidence: 99%

Section: 21mentioning

confidence: 99%

See 2 more Smart Citations

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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“…Many such longsarcomere muscles are highly extensible and undergo considerable changes in sarcomere length during isotonic contraction, in situ, which may involve alteration in filament organization. For example, at their longer lengths, the sarcomeres of Limulus telson and slow crustacean fibers frequently display A-bands with jagged boundaries due to misalignment of thick filaments (4,19,21). At the shortest in situ sarcomerelengths barnacle thick filaments have been observed to penetrate the Z-bands and enter neighboring sarcomeres (23), while Limulus thick filaments have been reported to decrease in length (3-6).…”

mentioning

confidence: 99%

Structure and paramyosin content of tarantula thick filaments.

Levine¹,

Kensler²,

Reedy³

et al. 1983

The Journal of Cell Biology

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Muscle fibers of the tarantula femur exhibit structural and biochemical characteristics similar to those of other Iong-sarcomere invertebrate muscles, having long A-bands and long thick filaments. 9-12 thin filaments surround each thick filament. Tarantula muscle has a paramyosin:myosin heavy chain molecular ratio of 0.31 _ 0.079 SD. We studied the myosin cross-bridge arrangement on the surface of tarantula thick filaments on isolated, negatively stained, and unidirectionally metal-shadowed specimens by electron microscopy and optical diffraction and filtering and found it to be similar to that previously described for the thick filaments of muscle of the closely related chelicerate arthropod, Limulus. Cross-bridges are disposed in a four-stranded right-handed helical arrangement, with 14.5-nm axial spacing between successive levels of four bridges, and a helical repeat period every 43.5 nm, The orientation of cross-bridges on the surface of tarantula filaments is also likely to be very similar to that on Limulus filaments as suggested by the similarity between filtered images of the two types of filaments and the radial distance of the centers of mass of the cross-bridges from the surfaces of both types of filaments. Tarantula filaments, however, have smaller diameters than Limulus fi.laments, contain less paramyosin, and display structure that probably reflects the organization of the filament backbone which is not as apparent in images of Limulus filaments. We suggest that the similarities between Limulus and tarantula thick filaments may be governed, in part, by the close evolutionary relationship of the two species.Using a modified isolation procedure and improved electron microscopic techniques together with computer image and optical diffraction analyses, we recently described the structure of the myosin cross-bridge arrangement on the surface of negatively stained thick filaments isolated from unstimulated Limulus telson levator muscle (15,22,30). Four crossbridges extend from the surface of these filaments at each level, with an axial rise of 14.5 nm between adjacent levels and a helical repeat period of 43.5 nm, as predicted by Wray et al. (36) and confirmed by computer image reconstruction (30). Furthermore, by unidirectional metal-shadowing we determined that the myosin cross-bridges are disposed in a major right-handed helix, having 12 subunits per complete turn (175 nm), on the filament surface (16).Wray (35) recently reported that the x ray patterns from glycerinated, relaxed tarantula leg muscle resemble those he earlier obtained from similar preparations of Limulus muscle (36). Here we present the results of an electron microscopic, optical diffraction, and biochemical analysis of the structure and paramyosin content, respectively, of thick filaments from tarantula femur muscle fibers and compare them with those from our previous analysis of Limulus telson muscle thick filaments (15,16,22,30). MATERIALS AND METHODSTarantula (Eurypelma sp.) specimens (sex unknown) were purchased from C...

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Complete amino acid sequence ofMytilus anterior byssus retractor paramyosin and its putative phosphorylation site

et al. 2000

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A cDNA encoding the full‐length paramyosin molecule was cloned from the mussel Mytilus galloprovincialis, a species closely related to Mytilus edulis. It contained 3,497 nucleotides (nt), with 79 and 826 nt for the 5′ and 3′ non‐coding regions, respectively. The coding region was composed of 2,592 nt for 864 amino acid residues, a size typical of paramyosin. While genomic DNA digests with either HindIII or PstI exhibited a single band when hybridized with a SacI fragment of paramyosin cDNA, the digests with either EcoRV or EcoRI showed two bands, suggesting that the mussel has at least two genes encoding paramyosin. The mRNAs encoding paramyosin were most abundant in muscle tissues from byssus retractor and adductor muscles. Only traces of paramyosin transcripts were found in the tissue of foot, gill, inner mantle, and outer mantle. The same phosphorylatable peptide previously reported for paramyosin from the bivalve Mercenaria mercenaria, Ser‐Arg‐Ser‐Met‐Ser(P)‐Val‐Ser‐Arg (Watabe et al. 1989. Comp Biochem Physiol 94B:813–821) was found in the C‐terminal non‐helical part of this Mytilus paramyosin. We predict that this particular paramyosin has a coiled‐coil structure composed of two α‐helices that show the heptad repeats (a‐b‐c‐d‐e‐f‐g) with further 28‐amino acid repeat zones, where a and d tend to be occupied by nonpolar residues. J. Exp. Zool. 286:24–35, 2000.© 2000 Wiley‐Liss, Inc.

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Paramyosin in invertebrate muscles. II. Content in relation to structure and function.

Cited by 109 publications

References 26 publications

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

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

Structure and paramyosin content of tarantula thick filaments.

Complete amino acid sequence ofMytilus anterior byssus retractor paramyosin and its putative phosphorylation site

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