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Science 5 August 2005:
Vol. 309. no. 5736, pp. 941 - 943
DOI: 10.1126/science.1114347
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Reports

Export-Mediated Assembly of Mycobacterial Glycoproteins Parallels Eukaryotic Pathways

Brian C. VanderVen, Jeffery D. Harder, Dean C. Crick, John T. Belisle*

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.

Mycobacteria Research Laboratories, Department of Microbiology, Immunology, and Pathology, Colorado State University, Fort Collins, CO 80523–1682, USA.

* To whom correspondence should be addressed. E-mail: jbelisle{at}colostate.edu

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O-Mannosylation is Required for Degradation of the Endoplasmic Reticulum-associated Degradation Substrate Gas1*p via the Ubiquitin/Proteasome Pathway in Saccharomyces cerevisiae.
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New Insights into the Biosynthesis of Mycobacterial Lipomannan Arising from Deletion of a Conserved Gene.
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Membrane association is a determinant for substrate recognition by PMT4 protein O-mannosyltransferases.
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Physical and Functional Association of Human Protein O-Mannosyltransferases 1 and 2.
K. Akasaka-Manya, H. Manya, A. Nakajima, M. Kawakita, and T. Endo (2006)
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Science. ISSN 0036-8075 (print), 1095-9203 (online)