Export-mediated assembly of mycobacterial glycoproteins parallels eukaryotic pathways.

Abstract

Protein O-mannosylation is an essential and evolutionarily conserved post-translational modification among eukaryotes. This form of protein modification is also described in Mycobacterium tuberculosis; however, the mechanism of mannoprotein assembly remains unclear. Evaluation of differentially translocated chimeric proteins and mass spectrometry to monitor glycosylation demonstrated that specific translocation processes were required for protein O-mannosylation in M. tuberculosis. Additionally, Rv1002c, a M. tuberculosis membrane protein homolog of eukaryotic protein mannosyltransferases, was shown to catalyze the initial step of protein mannosylation. Thus, the process of protein mannosylation is conserved between M. tuberculosis and eukaryotic organisms.

• Authors: Brian C VanderVen, Jeffery D Harder, Dean C Crick, John T Belisle
• Journal: Science (New York, N.Y.) (Science) Vol. 309 Issue 5736 Pg. 941-3 (Aug 05 2005) ISSN: 1095-9203 [Electronic] United States
• PMID: 16081738 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Membrane Glycoproteins
• Recombinant Fusion Proteins
• mannoproteins
• Mannosyltransferases
• protein O-mannosyltransferase
• Mannose

Topics

• Cloning, Molecular
• Eukaryotic Cells (metabolism)
• Evolution, Molecular
• Glycosylation
• Mannose (metabolism)
• Mannosyltransferases (metabolism)
• Membrane Glycoproteins (genetics, metabolism)
• Mycobacterium smegmatis (genetics)
• Mycobacterium tuberculosis (genetics, metabolism)
• Protein Processing, Post-Translational
• Protein Transport
• Recombinant Fusion Proteins (metabolism)