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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.

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

Brian H. Lower and Peter J. Kennelly*

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.


* Corresponding author. Mailing address: Department of Biochemistry-0308, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061. Phone: (540) 231-4317. Fax: (540) 231-9070. E-mail: pjkennel{at}vt.edu.


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.




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