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Tuberculosis
Volume 91, Issue 6
, Pages 544-548
, November 2011
Expression of OmpATb is dependent on small membrane proteins in Mycobacterium bovis BCG
References
- . The envelope of mycobacteria. Annu Rev Biochem. 1995;64:29–63
- . Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure. Proc Natl Acad Sci U S A. 2008;105:3963–3967
- . Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state. J Bacteriol. 2008;190:5672–5680
- . Direct visualization by cryo-EM of the mycobacterial capsular layer: a labile structure containing ESX-1-secreted proteins. PLoS Pathog. 2010;6:e1000794
- . Mycobacterial outer membranes: in search of proteins. Trends Microbiol. 2010;18:109–116
- . Expression of a gene for a porin-like protein of the OmpA family from Mycobacterium tuberculosis H37Rv. J Bacteriol. 1998;180:3541–3547
- . Mycobacterium tuberculosis Rv0899 adopts a mixed alpha/beta-structure and does not form a transmembrane beta-barrel. Biochemistry. 2010;49:2768–2777
- Yang Y, Auguin D, Delbecq S, Dumas E, Molle G, Molle V, et al. Structure of the Mycobacterium tuberculosis OmpATb protein: a model of an oligomeric channel in the mycobacterial cell wall. Proteins; 79: 645–661.
- pH-dependent pore-forming activity of OmpATb from Mycobacterium tuberculosis and characterization of the channel by peptidic dissection. Mol Microbiol. 2006;61:826–837
- . The N-terminal domain of OmpATb is required for membrane translocation and pore-forming activity in mycobacteria. J Bacteriol. 2007;189:6351–6358
- The functions of OmpATb, a pore-forming protein of Mycobacterium tuberculosis. Mol Microbiol. 2002;46:191–201
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998;393:537–544
- . Hydrophobic peptides: novel regulators within bacterial membrane. Mol Microbiol. 2009;72:5–11
- Temperature-dependent regulation of mycolic acid cyclopropanation in saprophytic mycobacteria: role of the Mycobacterium smegmatis 1351 gene (MSMEG_1351) in cis-cyclopropanation of alpha-mycolates. J Biol Chem. 2010;285:21698–21707
- Specialized transduction: an efficient method for generating marked and unmarked targeted gene disruptions in Mycobacterium tuberculosis, M. bovis BCG and M. smegmatis. Microbiology. 2002;148:3007–3017
- . Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol. 2003;48:77–84
- . On the killing of mycobacteria by macrophages. Cell Microbiol. 2008;10:529–548
- Rv0901 from Mycobacterium tuberculosis, a possible novel virulent gene proved through the recombinant Mycobacterium smegmatis. Jpn J Infect Dis. 2009;62:26–31
- . pETPhos: a customized expression vector designed for further characterization of Ser/Thr/Tyr protein kinases and their substrates. Plasmid. 2008;60:149–153
- . The complexities of porin genetic regulation. J Mol Microbiol Biotechnol. 2010;18:24–36
- . Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev. 2007;21:2473–2484
- . A molecular Swiss army knife: OmpA structure, function and expression. FEMS Microbiol Lett. 2007;273:1–11
- Expression of the ompATb operon accelerates ammonia secretion and adaptation of Mycobacterium tuberculosis to acidic environments. Mol Microbiol. 2011;80:900–918
- . Mycobacterial mutants with defective control of phagosomal acidification. PLoS Pathog. 2005;1:269–278
PII: S1472-9792(11)00124-7
doi: 10.1016/j.tube.2011.06.008
© 2011 Elsevier Ltd. All rights reserved.
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Tuberculosis
Volume 91, Issue 6
, Pages 544-548
, November 2011
