Structure and functions of tropomyosins from muscle and non-muscle sources

Smillie, Lawrence B.

doi:10.1016/0968-0004(79)90003-3

Cited by 221 publications

(122 citation statements)

References 17 publications

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“…We SNP mapped the rg1 mutation to the right arm of linkage group 1, near the gene lev-11 (Wicks et al, 2001). lev-11 encodes the worm homolog of tropomyosin, a thin filament muscle protein that is involved in Ca 2ϩ regulation of muscle contraction (Smillie, 1979;Taylor, 1979;Ohtsuki et al, 1986;Kagawa et al, 1995). When we separated the rg1 mutation away from unc-103(sy557), we noted that the rg1 mutation confers phenotypes similar to lev-11(x12) mutants (Lewis et al, 1980;Kagawa et al, 1995).…”

Section: Spicule Protraction Mutants Vary In Their Penetrance and Resmentioning

confidence: 99%

Integration of Male Mating and Feeding Behaviors inCaenorhabditis elegans

Gruninger¹,

Gualberto²,

LeBoeuf³

et al. 2006

J. Neurosci.

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The Caenorhabditis elegans male must integrate various environmental cues to ensure proper execution of mating. One step of male mating, the insertion of the male copulatory spicules into its mate, requires UNC-103 ERG (ether-a-go-go-related gene)-like K ϩ channels. unc-103(lf) alleles cause males to protract their spicules spontaneously in the absence of mating cues. To identify proteins that work with UNC-103, we suppressed unc-103(lf) and isolated lev-11(rg1). LEV-11 (tropomyosin) regulates the spicules directly by controlling the male sex muscles and indirectly by controlling the pharyngeal muscles. lev-11-mediated suppression requires the pharyngeal NSM neurosecretory motor neurons; ablating these neurons in lev-11(rg1); unc-103(lf) males restores spontaneous spicule protraction. Additionally, unc-103-induced spicule protraction can be suppressed by reducing a pharyngeal-specific troponin T. These observations demonstrate that non-genitalia cells involved in feeding also mediate male sexual behaviors.

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Section: Spicule Protraction Mutants Vary In Their Penetrance and Resmentioning

confidence: 99%

Integration of Male Mating and Feeding Behaviors inCaenorhabditis elegans

Gruninger¹,

Gualberto²,

LeBoeuf³

et al. 2006

J. Neurosci.

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“…In skeletal muscle, the function of tropomyosin is in association with the troponin complex (troponin I, T, and C) to regulate the calcium-sensitive interaction of actin and myosin (87,94).…”

Section: Beta-tropomyosin and Fibroblast Tropomyosin 1 Cdnas Wementioning

confidence: 99%

“…In striated muscle, tropomyosin is localized to the thin filaments, where it is found along both grooves of the actin filaments (87). The function of tropomyosin in skeletal and cardiac muscle is in association with the troponin complex (troponin I, T, and C) to regulate the calcium-sensitive interaction of actin and myosin (87,94).…”

mentioning

confidence: 99%

“…Although they are present in all cells, different forms of the protein are characteristic of specific cell types. Tropomyosin is a rodlike protein composed of two highly alpha-helical subunits wrapped around each other to form a coiled-coil structure (87). Skeletal muscle contains two forms of tropomyosin termed alpha and beta, the proportions of which vary with fiber type (9,10,19,20,81,88).…”

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confidence: 99%

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Nonmuscle and muscle tropomyosin isoforms are expressed from a single gene by alternative RNA splicing and polyadenylation.

Helfman¹,

Cheley²,

Kuismanen³

et al. 1986

Mol. Cell. Biol.

175

122

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The molecular basis for the expression of rat embryonic fibroblast tropomyosin 1 and skeletal muscle beta-tropomyosin was determined. cDNA clones encoding these tropomyosin isoforms exhibit complete identity except for two carboxy-proximal regions (amino acids 189 to 213 and 258 to 284) and different 3'-untranslated sequences. The isoform-specific regions delineate the troponin T-binding domains of skeletal muscle tropomyosin. Analysis of genomic clones indicates that there are two separate loci in the rat genome that contain sequences complementary to these mRNAs. One locus is a pseudogene. The other locus contains a single gene made up of 11 exons and spans approximately 10 kilobases. Sequences common to all mRNAs were found in exons 1 through 5 (amino acids 1 to 188) and exons 8 and 9 (amino acids 214 to 257). Exons 6 and 11 are specific for fibroblast mRNA (amino acids 189 to 213 and 258 to 284, respectively), while exons 7 and 10 are specific for skeletal muscle mRNA (amino acids 189 to 213 and 258 to 284, respectively). In addition, exons 10 and 11 each contain the entire 3'-untranslated sequences of the respective mRNAs including the polyadenylation site. Although the gene is also expressed in smooth muscle (stomach, uterus, and vas deferens), only the fibroblast-type splice products can be detected in these tissues. S1 and primer extension analyses indicate that all mRNAs expressed from this gene are transcribed from a single promoter. The promoter was found to contain G-C-rich sequences, a TATA-like sequence TTTTA, no identifiable CCAAT box, and two putative Sp1-binding sites.

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“…Interaction des sous unités dans la tropomyosine native d'après [30]. La tropomyosine native est assemblée à partir de deux sous unités identiques ou différentes.…”

Section: Trop Omyosines Du Tissu Musculaireunclassified