Phosphorylation of the N-terminal region of Caenorhabditis elegans paramyosin.
Paramyosin from Caenorhabditis elegans was examined for post-translational modification by phosphorylation. Paramyosin purified from populations of mixed-age animals contained 0.7 to 2.0 moles of phosphate per mole of paramyosin. Paramyosin was also phosphorylated in vitro by an endogenous kinase in the particulate fraction. 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. 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. 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.
Department of Genetics, Washington University, St. Louis, MO 63110.
L A
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Schriefer
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Waterson
D000595:Amino Acid Sequence; D000596:Amino Acids; D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D002107:Caenorhabditis / Q000378:metabolism*; D008969:Molecular Sequence Data; D010766:Phosphorylation; D014335:Tropomyosin / Q000378:metabolism*
D000596:Amino Acids; D001426:Bacterial Proteins; D014335:Tropomyosin