This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Mescher, M. F. Articles by Watson, S. W. Search for Related Content PubMed PubMed Citation Articles by Mescher, M. F. Articles by Watson, S. W.

Protein and Carbohydrate Composition of the Cell Envelope of Halobacterium salinarium¹

^a The Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138, and Woods Hole Oceanographic Institution, Woods Hole, Massachusetts 02543

ABSTRACT

The isolated cell envelope of Halobacterium salinarium strain 1 contained 15 to 20 proteins that were resolved by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. All but one of these proteins had molecular weights of 130,000 or less and together accounted for 50 to 60% of the total envelope protein. The remaining 40 to 50% of the envelope protein was accounted for by a single protein with an apparent molecular weight of approximately 194,000 that stained for carbohydrate with periodate-Schiff reagent. The proteolytic enzymes trypsin and Pronase were used to show that the carbohydrate is covalently bound to the protein. Separation of amino sugar- and hexose-containing tryptic peptides by gel filtration indicated that all of the nonlipid carbohydrate of the cell envelope is covalently bound to protein. The results of partial purification by phenol extraction indicated that both the amino sugar and hexose are bound to the 194,000-molecular-weight protein. Exposure of isolated cell envelopes to low salt concentration resulted in solubilization of a majority of the envelope proteins. A relatively small number of proteins, including the high-molecular-weight, carbohydrate-containing protein, remained bound to the sedimentable cell membrane fraction.

¹ Contribution no. 3356 from the Woods Hole Oceanographic Institution.

This article has been cited by other articles:

• Shams-Eldin, H., Chaban, B., Niehus, S., Schwarz, R. T., Jarrell, K. F. (2008). Identification of the Archaeal alg7 Gene Homolog (Encoding N-Acetylglucosamine-1-Phosphate Transferase) of the N-Linked Glycosylation System by Cross-Domain Complementation in Saccharomyces cerevisiae. J. Bacteriol. 190: 2217-2220 [Abstract] [Full Text]  
• Horzempa, J., Dean, C. R., Goldberg, J. B., Castric, P. (2006). Pseudomonas aeruginosa 1244 Pilin Glycosylation: Glycan Substrate Recognition.. J. Bacteriol. 188: 4244-4252 [Abstract] [Full Text]  
• Horzempa, J., Comer, J. E., Davis, S. A., Castric, P. (2006). Glycosylation Substrate Specificity of Pseudomonas aeruginosa 1244 Pilin. J. Biol. Chem. 281: 1128-1136 [Abstract] [Full Text]  
• Smedley, J. G. III, Jewell, E., Roguskie, J., Horzempa, J., Syboldt, A., Stolz, D. B., Castric, P. (2005). Influence of Pilin Glycosylation on Pseudomonas aeruginosa 1244 Pilus Function. Infect. Immun. 73: 7922-7931 [Abstract] [Full Text]  
• Kikuchi, A., Sagami, H., Ogura, K. (1999). Evidence for Covalent Attachment of Diphytanylglyceryl Phosphate to the Cell-surface Glycoprotein of Halobacterium halobium. J. Biol. Chem. 274: 18011-18016 [Abstract] [Full Text]