The Membrane-Associated Protein-Serine/Threonine Kinase from Sulfolobus solfataricus Is a Glycoprotein

AUTOR(ES)

Lower, Brian H.

FONTE

American Society for Microbiology

RESUMO

Treatment of a sodium dodecyl sulfate-polyacrylamide gel with periodic acid-Schiff (PAS) stain or blotting with Galanthus nivalis agglutinin revealed the presence of several glycosylated polypeptides in a partially purified detergent extract of the membrane fraction of Sulfolobus solfataricus. One of the glycoproteins comigrated with the membrane-associated protein-serine/threonine kinase from S. solfataricus, which had been radiolabeled by autophosphorylation with [32P]ATP in vitro. Treatment with a chemical deglycosylating agent, trifluoromethanesulfonic acid, abolished PAS staining and reduced the Mr of the protein kinase from ∼67,000 to ∼62,000. Protein kinase activity also adhered to, and could be eluted from, agarose beads containing bound G. nivalis agglutinin. Glycosylation of the protein kinase implies that at least a portion of this integral membrane protein resides on the external surface of the cell membrane.

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