Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1828, Issue 3, Pages 938-943Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2012.11.023
Keywords
Archaea; Haloferax volcanii; Lipid modification; Membrane protein; S-layer glycoprotein
Categories
Funding
- Israel Science Foundation [8/11]
- US Army Research Office [W911NF-11-1-520]
- LIPID MAPS Large Scale Collaborative from NIH [GM-069338]
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The S-layer glycoprotein is the sole component of the protein shell surrounding Haloferax volcanii cells. The deduced amino acid sequence of the S-layer glycoprotein predicts the presence of a C-terminal membrane-spanning domain. However, several earlier observations, including the ability of EDTA to selectively solubilize the protein, are inconsistent with the presence of a trans-membrane sequence. In the present report, sequential solubilization of the S-layer glycoprotein by EDTA and then with detergent revealed the existence of two distinct populations of the S-layer glycoprotein. Whereas both S-layer glycoprotein populations underwent signal peptide cleavage and N-glycosylation, base hydrolysis followed by mass spectrometry revealed that a lipid, likely archaetidic acid, modified only the EDTA-solubilized version of the protein. These observations are consistent with the S-layer glycoprotein being initially synthesized as an integral membrane protein and subsequently undergoing a processing event in which the extracellular portion of the protein is separated from the membrane-spanning domain and transferred to a waiting lipid moiety. (C) 2012 Elsevier B.V. All rights reserved.
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