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unc-15  -  Protein UNC-15

Caenorhabditis elegans

 
 
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Disease relevance of paramyosin

 

High impact information on paramyosin

  • Mutant embryos in which cleavage arrests prematurely also generate cells that produce myosin and paramyosin [3].
  • Specific antibodies to myosin and paramyosin, major protein constituents of differentiated muscle, react with mesodermal cells in wild-type embryos towards the end of the first half of embryogenesis [3].
  • In CB1214 mutants where paramyosin is absent, beta-filagenin assembled with myosin to form abnormal tubular filaments with a periodicity identical to wild type [4].
  • Within these regions, MHC A displays a more hydrophobic rod surface, making it more similar to paramyosin, which forms the thick filament core [5].
  • The organization of myosin heavy chains (mhc) A and B and paramyosin (pm) which are the major proteins of thick filaments in adult wild-type Caenorhabditis elegans were studied during embryonic development [6].
 

Biological context of paramyosin

  • All three regions contain three copies of a Ser-*-Ser-*-Ala motif, the most likely target for phosphorylation in paramyosin, suggesting that these regions may be modified by the same kinase [7].
  • The Caenorhabditis elegans paramyosin gene (unc-15) was identified by screening with specific antibodies an "exon-expression" library containing lacZ/nematode gene fusions [1].
  • Analysis of the in vitro phosphorylated paramyosin in comparison with the DNA sequence of the unc-15 paramyosin gene of C. elegans shows that serine residues in the non-alpha-helical N-terminal region are the targets of the kinase [7].
  • Myosin isoforms A and B are located at the surface of the central and polar regions, respectively, of thick filaments in body muscle cells of Caenorhabditis elegans, whereas paramyosin and a distinct core structure comprise the backbones of these filaments [8].
  • Prior studies have shown that such immunization stimulates a much stronger antibody response to recombinant and native filarial paramyosin than that seen after normal infection [9].
 

Anatomical context of paramyosin

  • Myosin heavy chains A and B and paramyosin proteins appear to be compatible with functionally and structurally distinct muscle cell types that arise by multiple developmental pathways [10].
  • By polarized light microscopy of body wall muscle, unc-96 mutants display reduced myofibrillar organization and characteristic birefringent "needles." By immunofluorescent staining of known myofibril components, unc-96 mutants show major defects in the organization of M-lines and in the localization of a major thick filament component, paramyosin [11].
  • A region of the myosin rod important for interaction with paramyosin in Caenorhabditis elegans striated muscle [12].
  • In the present study, we demonstrate the B cell epitope of paramyosin recognized by SJ18 epsilon [13].
  • The thick (myosin) myofilaments show a variable length (from 2.2 microns up to 6 microns) and width (from 14 nm up to 231 nm) and contain a central core of paramyosin, which is absent in vertebrate muscles [14].
 

Associations of paramyosin with chemical compounds

  • Here we describe the structure of the gene coding for the paramyosin of T. solium [15].
  • Several leucine zippers are located on the hydrophobic face of the alpha-helix in paramyosin which, together with disulfide bonds between cysteines, are probably involved in the stabilization of the dimer [16].
  • We have characterized 20 ethyl methanesulfonate-induced mutations in essential genes closely linked to unc-15 [17].
 

Physical interactions of paramyosin

  • The major paramyosin species interacts with the two genetically specified myosin heavy chain isoforms [18].
 

Regulatory relationships of paramyosin

  • In mutants that do not express MHC B or that express defective paramyosin, muscle structure is disrupted and movement is impaired [19].
 

Other interactions of paramyosin

  • The N-terminal region of paramyosin has significant similarity to the non-helical C-terminal region of the two body wall myosin heavy chains of C. elegans [7].
  • Similar calculations suggest optimal interactions between paramyosin molecules and myosin rods and in their anti-parallel alignments [1].
  • The six proteins also cosedimented with thick filaments purified by gradient centrifugation from CB190 mutants lacking myosin heavy chain B and from CB1214 mutants lacking paramyosin [20].
  • The suppression pattern of the suppressor against the two muscle-affecting genes, unc-15 and unc-52, suggested that either the suppressors are expressed in a developmental stage-specific manner or that the unc-52 products are expressed in cell-types other than muscle, possibly hypodermis [21].
  • In the 0.65 map-unit interval around unc-15 defined by dpy-14 and unc-56, seven newly identified genes have been mapped relative to five existing genes [17].
 

Analytical, diagnostic and therapeutic context of paramyosin

References

  1. Paramyosin gene (unc-15) of Caenorhabditis elegans. Molecular cloning, nucleotide sequence and models for thick filament structure. Kagawa, H., Gengyo, K., McLachlan, A.D., Brenner, S., Karn, J. J. Mol. Biol. (1989) [Pubmed]
  2. Filarial paramyosin: cDNA sequences from Dirofilaria immitis and Onchocerca volvulus. Limberger, R.J., McReynolds, L.A. Mol. Biochem. Parasitol. (1990) [Pubmed]
  3. Muscle differentiation in normal and cleavage-arrested mutant embryos of Caenorhabditis elegans. Gossett, L.A., Hecht, R.M., Epstein, H.F. Cell (1982) [Pubmed]
  4. beta-Filagenin, a newly identified protein coassembling with myosin and paramyosin in Caenorhabditis elegans. Liu, F., Bauer, C.C., Ortiz, I., Cook, R.G., Schmid, M.F., Epstein, H.F. J. Cell Biol. (1998) [Pubmed]
  5. Hydrophobicity variations along the surface of the coiled-coil rod may mediate striated muscle myosin assembly in Caenorhabditis elegans. Hoppe, P.E., Waterston, R.H. J. Cell Biol. (1996) [Pubmed]
  6. Myosin and paramyosin of Caenorhabditis elegans embryos assemble into nascent structures distinct from thick filaments and multi-filament assemblages. Epstein, H.F., Casey, D.L., Ortiz, I. J. Cell Biol. (1993) [Pubmed]
  7. Phosphorylation of the N-terminal region of Caenorhabditis elegans paramyosin. Schriefer, L.A., Waterson, R.H. J. Mol. Biol. (1989) [Pubmed]
  8. The alteration of myosin isoform compartmentation in specific mutants of Caenorhabditis elegans. Epstein, H.F., Ortiz, I., Mackinnon, L.A. J. Cell Biol. (1986) [Pubmed]
  9. Vaccination with recombinant filarial paramyosin induces partial immunity to Brugia malayi infection in jirds. Li, B.W., Chandrashekar, R., Weil, G.J. J. Immunol. (1993) [Pubmed]
  10. Immunochemical localization of myosin heavy chain isoforms and paramyosin in developmentally and structurally diverse muscle cell types of the nematode Caenorhabditis elegans. Ardizzi, J.P., Epstein, H.F. J. Cell Biol. (1987) [Pubmed]
  11. Caenorhabditis elegans UNC-96 is a new component of M-lines that interacts with UNC-98 and paramyosin and is required in adult muscle for assembly and/or maintenance of thick filaments. Mercer, K.B., Miller, R.K., Tinley, T.L., Sheth, S., Qadota, H., Benian, G.M. Mol. Biol. Cell (2006) [Pubmed]
  12. A region of the myosin rod important for interaction with paramyosin in Caenorhabditis elegans striated muscle. Hoppe, P.E., Waterston, R.H. Genetics (2000) [Pubmed]
  13. The B cell epitope of paramyosin recognized by a protective monoclonal IgE antibody to Schistosoma japonicum. Nara, T., Tanabe, K., Mahakunkijcharoen, Y., Osada, Y., Matsumoto, N., Kita, K., Kojima, S. Vaccine (1997) [Pubmed]
  14. Ultrastructure of invertebrate muscle cell types. Paniagua, R., Royuela, M., García-Anchuelo, R.M., Fraile, B. Histol. Histopathol. (1996) [Pubmed]
  15. Gene structure of Taenia solium paramyosin. Vargas-Parada, L., Laclette, J.P. Parasitol. Res. (2003) [Pubmed]
  16. Drosophila melanogaster paramyosin: developmental pattern, mapping and properties deduced from its complete coding sequence. Vinós, J., Maroto, M., Garesse, R., Marco, R., Cervera, M. Mol. Gen. Genet. (1992) [Pubmed]
  17. Genetic organization of the region around UNC-15 (I), a gene affecting paramyosin in Caenorhabditis elegans. Rose, A.M., Baillie, D.L. Genetics (1980) [Pubmed]
  18. Assemblases and coupling proteins in thick filament assembly. Liu, F., Barral, J.M., Bauer, C.C., Ortiz, I., Cook, R.G., Schmid, M.F., Epstein, H.F. Cell Struct. Funct. (1997) [Pubmed]
  19. Myosin heavy chain gene amplification as a suppressor mutation in Caenorhabditis elegans. Maruyama, I.N., Miller, D.M., Brenner, S. Mol. Gen. Genet. (1989) [Pubmed]
  20. Purified thick filaments from the nematode Caenorhabditis elegans: evidence for multiple proteins associated with core structures. Epstein, H.F., Berliner, G.C., Casey, D.L., Ortiz, I. J. Cell Biol. (1988) [Pubmed]
  21. Genetic and molecular analysis of eight tRNA(Trp) amber suppressors in Caenorhabditis elegans. Kondo, K., Makovec, B., Waterston, R.H., Hodgkin, J. J. Mol. Biol. (1990) [Pubmed]
  22. Construction of Onchocerca volvulus cDNA libraries and partial characterization of the cDNA for a major antigen. Donelson, J.E., Duke, B.O., Moser, D., Zeng, W.L., Erondu, N.E., Lucius, R., Renz, A., Karam, M., Flores, G.Z. Mol. Biochem. Parasitol. (1988) [Pubmed]
  23. Analysis of Drosophila paramyosin: identification of a novel isoform which is restricted to a subset of adult muscles. Becker, K.D., O'Donnell, P.T., Heitz, J.M., Vito, M., Bernstein, S.I. J. Cell Biol. (1992) [Pubmed]
 
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