Beta-thymosins from marine invertebrates: primary structure and interaction with actin.

The beta-thymosins are distributed throughout the vertebrate phyla, and all known vertebrate beta-thymosins bind actin monomers. To determine whether beta-thymosin-like peptides function as actin-binding proteins in invertebrates, we fractionated perchloric acid extracts of the gonads of both the sea urchin, Arbacia punctulata, and the scallop, Argopecten irradians, and screened the fractions for proteins which could be crosslinked to actin. In each case a peptide was isolated which crosslinks to actin from both rabbit skeletal muscle and scallop cross-striated adductor muscle; both peptides were sequenced and each was found to consist of 40 amino acid residues, compared with 41-43 residues for the vertebrate beta-thymosins. The sequences of the scallop and sea urchin beta-thymosins are 80% identical to each other, 75% identical to residues 1-40 of thymosin beta4, and 72-80% identical to residues 1-40 of other vertebrate beta-thymosins. The sea urchin peptide was found to inhibit actin polymerization and nucleotide exchange. The affinity of the sea urchin peptide for rabbit muscle actin is apparently lower than that of thymosin beta4, since about twice the concentration of sea urchin peptide is required to give inhibition of actin polymerization or nucleotide exchange equivalent to thymosin beta4.