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The 38000-Mr poly(A)-binding protein of non-polysomal messenger ribonucleoproteins of cryptobiotic gastrulae of Artemia salina
De Herdt, E.; Piot, E.; Kondo, M.; Slegers, H. (1982). The 38000-Mr poly(A)-binding protein of non-polysomal messenger ribonucleoproteins of cryptobiotic gastrulae of Artemia salina. Eur. J. Biochem. 122(3): 453-460. hdl.handle.net/10.1111/j.1432-1033.1982.tb06459.x
In: European Journal of Biochemistry. Springer: Berlin. ISSN 0014-2956, more
Peer reviewed article  

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  • De Herdt, E.
  • Piot, E.
  • Kondo, M.
  • Slegers, H.

Abstract
    The 38000-Mr poly(A)-binding protein has been purified to near homogeneity from non-polysomal messenger ribonucleoprotein of Artemia salina [Slegers, H., De Herdt, E., and Kondo, M. (1981) Eur. J. Biochem. 117, 111-120]. The protein consists of approximately 357 amino acids and is characterized by a high glycine content of 22.5% and the presence of dimethylarginine. From polynucleotide-protein binding experiments a stoichiometry of 9–11 adenylate and 10–12 uridylate residues per protein molecule is calculated. The polypeptide is devoid of poly(A) polymerase and RNase activities. The poly(A)-binding protein and the helix-destabilizing protein HD40 [Marvil, D. K., Nowak, L., and Szer, W. (1980) J. Biol. Chem. 255, 6466–6472] have the same mobility in polyacrylamide/dodecylsulphate gel electrophoresis and exhibit a comparable amino acid composition and protein-polynucleotide stoichiometry. Based on the length of poly(A) sequences of mRNA and from protein-poly(A) binding experiments, a repetitive binding of the 38000-Mr protein on the poly(A) sequence is demonstrated. The 38000-Mr protein of cytoplasmic and membrane-bound non-polysomal messenger ribonucleoproteins is also compared.

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