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

Abstract

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 alpha-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.

Isolation and characterization of a novel 45 kDa calponin-like protein from anterior byssus retractor muscle of the mussel Mytilus galloprovincialis

“…Two‐dimensional electrophoresis using an agarose gel for isoelectric focusing was adopted to detect proteins that constitute ABRM myofibrils. It showed major spots of myofibrillar proteins including myosin heavy chain, 17 paramyosin, 18 catchin, 19 actin, 17 tropomyosin, 20 and myosin light chains, 21 together with aggregated paramyosin, 18 as shown in Fig. 1.…”

Paramyosin from the Disc Abalone Haliotis Discus Discus

“…For comparison, the amino acid sequences of paramyosins from four species of invertebrates, Mediterranean mussel M. galloprovincialis (Watabe et al . ), European house dust mite Dermatophagoides pteronyssinus (Lee et al . ), storage mite Blomia tropicalis (Ramos et al .…”

“…Among edible invertebrates (mostly crustaceans and mollusks), Mediterranean mussel M. galloprovincialis is the only species with an elucidated paramyosin amino acid sequence (Watabe et al . ). Our previous inhibition immunoblotting data proved the IgE cross‐reactivity among molluscan paramyosins including those from disc abalone and Mediterranean mussel (Suzuki et al .…”

Thermally induced gelation of paramyosin from scallop adductor muscle

“…The paramyosin molecule isolated from mussel muscle contains seven cysteine residues per subunit chain 10 . The two reactive cysteine residues of the paramyosin subunit can be modified with maleimide–biotin and are located in pairs at the N ‐terminal end of the molecule and ∼ 30 nm from the C ‐terminal end 22 .…”

“…Myosin and paramyosin are closely related molecules that coassemble to form highly ordered thick filaments in invertebrate muscles. The paramyosin molecule is composed of two identical α‐helices that give it a coiled‐coil structure with short non‐helical extensions at both the N ‐ and C ‐termini 7–10 . The molar ratio of the two proteins varies greatly among muscle types, ranging from a large excess of paramyosin in some smooth muscles to a large excess of myosin in fast‐acting striated muscles 4,11 …”