Protein post-translational modifications in bacteria
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Immunology and Microbiology,Microbiology,Infectious Diseases
Link
http://www.nature.com/articles/s41579-019-0243-0.pdf
Reference169 articles.
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3. Faridmoayer, A., Fentabil, M. A., Mills, D. C., Klassen, J. S. & Feldman, M. F. Functional characterization of bacterial oligosaccharyltransferases involved in O-linked protein glycosylation. J. Bacteriol. 189, 8088–8098 (2007).
4. Nita-Lazar, M., Wacker, M., Schegg, B., Amber, S. & Aebi, M. The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. Glycobiology 15, 361–367 (2005).
5. Pearce, M. J., Mintseris, J., Ferreyra, J., Gygi, S. P. & Darwin, K. H. Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis. Science 322, 1104–1107 (2008). This is the first report of Pup in bacteria, linking its action to proteasome PafA and protein degradation in M. tuberculosis.
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