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Journal of Bacteriology, May 2002, p. 2614-2619, Vol. 184, No. 10
0021-9193/02/$04.00+0 DOI: 10.1128/JB.184.10.2614-2619.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061
Received 19 November 2001/ Accepted 26 February 2002
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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