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      Cloning of a full-length complementary DNA for an Artemia salina glycine-rich protein. Structural relationship with RNA binding proteins.

      The Journal of Biological Chemistry
      Amino Acid Sequence, Animals, Artemia, genetics, Base Sequence, Carrier Proteins, Cloning, Molecular, DNA, metabolism, Insect Proteins, Invertebrate Hormones, Molecular Sequence Data, Protein Conformation, RNA, RNA-Binding Proteins

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          Abstract

          Overlapping cDNAs have been isolated containing all the coding sequences for Artemia salina protein GRP33, a glycine-rich protein (16.6 mol % glycine), with a molecular weight of 32,992. GRP33 is closely related to HD40, the major protein component of Artemia heterogeneous nuclear ribonucleoprotein particles, and shares certain characteristics with other RNA binding proteins. The C-terminal region (123 amino acids) contains 39 glycine residues. This region has multiple arginine residues flanked by glycines, resembling the glycine-dimethylarginine clusters present in other RNA binding proteins. Secondary structure predictions for the protein reveal two distinct domains: a hydrophilic C-terminal domain with an extended conformation and a larger N-terminal domain with a number of alpha-helices and beta-sheets.

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