Complete amino acid sequence of PO protein in bovine peripheral nerve myelin

J Biol Chem. 1987 Mar 25;262(9):4208-14.

Abstract

The P0 protein is a major structural glycoprotein of molecular weight 28,000 in peripheral nerve myelin. The complete amino acid sequence of bovine P0 protein was determined. The polypeptide chain consists of 219 amino acid residues and includes a highly hydrophobic domain (residues 125-150) in the middle, which probably represents a transmembrane segment. The amino terminal domain (residues 1-124) is relatively hydrophobic, but contains a negatively charged carbohydrate chain at Asn93. This domain is most likely located on the extracellular side of the membrane and may contribute to formation of the myelin intraperiod line by hydrophobic and electrostatic interactions. On the other hand, the basic carboxyl-terminal domain (residues 151-219) may protrude from the cytoplasmic side of the membrane and is probably involved together with basic proteins in the formation of the major myelin dense line through electrostatic interaction with acidic lipids in the membrane. The few interspecies amino acid variations between the bovine P0 and the rat P0 sequences, deduced from the cDNA (Lemke, G., and Axel, R. (1985) Cell 40, 501-508), indicate that the P0 protein is conserved across species.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Cyanogen Bromide
  • Cytoplasm
  • Endopeptidases
  • Membrane Proteins
  • Myelin P0 Protein
  • Myelin Proteins* / isolation & purification
  • Myelin Sheath / analysis*
  • Peptide Fragments / isolation & purification
  • Peripheral Nerves / analysis*
  • Serine Endopeptidases*

Substances

  • Membrane Proteins
  • Myelin P0 Protein
  • Myelin Proteins
  • Peptide Fragments
  • Endopeptidases
  • Serine Endopeptidases
  • glutamyl endopeptidase
  • Cyanogen Bromide