Rhamnose Links Moonlighting Proteins to Membrane Phospholipid in Mycoplasmas
| Autor: | Runhua Liu, James M. Daubenspeck, Kevin Dybvig |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Protein moonlighting Hydrolases lcsh:Medicine Biochemistry Rhamnose Cell membrane chemistry.chemical_compound Mycoplasma Tandem Mass Spectrometry lcsh:Science Phospholipids Chromatography High Pressure Liquid Staining Multidisciplinary Esterases Reference Standards Lipids Enzymes Membrane Staining Chemistry medicine.anatomical_structure Phospholipases Physical Sciences Electrophoresis Polyacrylamide Gel Research Article Signal peptide Enolase Mollicutes Biology Research and Analysis Methods Gas Chromatography-Mass Spectrometry Phosphates 03 medical and health sciences Bacterial Proteins medicine Phospholipase D Amino Acid Sequence Cytoplasmic Staining Bacteria lcsh:R Cell Membrane Organisms Chemical Compounds Biology and Life Sciences Proteins Membrane Proteins Chaperone Proteins 030104 developmental biology chemistry Membrane protein Specimen Preparation and Treatment Phosphopyruvate Hydratase Enzymology lcsh:Q Peptidoglycan Peptides Protein Processing Post-Translational |
| Zdroj: | PLoS ONE PLoS ONE, Vol 11, Iss 9, p e0162505 (2016) |
| ISSN: | 1932-6203 |
| Popis: | Many proteins that have a primary function as a cytoplasmic protein are known to have the ability to moonlight on the surface of nearly all organisms. An example is the glycolytic enzyme enolase, which can be found on the surface of many types of cells from bacteria to human. Surface enolase is not enzymatic because it is monomeric and oligomerization is required for glycolytic activity. It can bind various molecules and activate plasminogen. Enolase lacks a signal peptide and the mechanism by which it attaches to the surface is unknown. We found that treatment of whole cells of the murine pathogen Mycoplasma pulmonis with phospholipase D released enolase and other common moonlighting proteins. Glycostaining suggested that the released proteins were glycosylated. Cytoplasmic and membrane-bound enolase was isolated by immunoprecipitation. No post-translational modification was detected on cytoplasmic enolase, but membrane enolase was associated with lipid, phosphate and rhamnose. Treatment with phospholipase released the lipid and phosphate from enolase but not the rhamnose. The site of rhamnosylation was identified as a glutamine residue near the C-terminus of the protein. Rhamnose has been found in all species of mycoplasma examined but its function was previously unknown. Mycoplasmas are small bacteria with have no peptidoglycan, and rhamnose in these organisms is also not associated with polysaccharide. We suggest that rhamnose has a central role in anchoring proteins to the membrane by linkage to phospholipid, which may be a general mechanism for the membrane association of moonlighting proteins in mycoplasmas and perhaps other bacteria. |
| Databáze: | OpenAIRE |
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