2011
DOI: 10.1371/journal.pone.0027475
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Identification and Localization of Myxococcus xanthus Porins and Lipoproteins

Abstract: Myxococcus xanthus DK1622 contains inner (IM) and outer membranes (OM) separated by a peptidoglycan layer. Integral membrane, β-barrel proteins are found exclusively in the OM where they form pores allowing the passage of nutrients, waste products and signals. One porin, Oar, is required for intercellular communication of the C-signal. An oar mutant produces CsgA but is unable to ripple or stimulate csgA mutants to develop suggesting that it is the channel for C-signaling. Six prediction programs were evaluate… Show more

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Cited by 25 publications
(29 citation statements)
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References 58 publications
(70 reference statements)
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“…Membrane fractionation indicated that CsgA is an inner membrane protein (Simunovic et al 2003), not an outer membrane protein as previously reported (Lobedanz and Sogaard-Andersen 2003). Extensive proteomic studies have likewise never placed CsgA in the outer membrane or on the cell surface (Kahnt et al 2010;Bhat et al 2011), and no receptor has ever been identified. The p17 form lacks the N-terminal NAD + -binding domain, and genomic replacement of a truncated csgA gene encoding an 18.1-kDa protein abolishes development (Lobedanz and Sogaard-Andersen 2003).…”
mentioning
confidence: 59%
“…Membrane fractionation indicated that CsgA is an inner membrane protein (Simunovic et al 2003), not an outer membrane protein as previously reported (Lobedanz and Sogaard-Andersen 2003). Extensive proteomic studies have likewise never placed CsgA in the outer membrane or on the cell surface (Kahnt et al 2010;Bhat et al 2011), and no receptor has ever been identified. The p17 form lacks the N-terminal NAD + -binding domain, and genomic replacement of a truncated csgA gene encoding an 18.1-kDa protein abolishes development (Lobedanz and Sogaard-Andersen 2003).…”
mentioning
confidence: 59%
“…5A), suggesting that this domain plays a critical A motility function. Prior proteomic studies found the CglD lipoprotein (MXAN_0962) in the inner membrane or OM and OM vesicles (OMVs) (2,13). These different findings may result from complex cell fractionation properties for a large protein that likely binds multiple factors.…”
Section: Discussionmentioning
confidence: 99%
“…If CsgA is an enzyme, its substrate and product remain to be identified. Interestingly, the outer membrane porin Oar is required for C signaling and has been proposed to be the channel for the export of the C signal (31). Cellular responses to C signaling involve FruA, which is similar to the response regulators of two-component signal transduction systems (32,33).…”
mentioning
confidence: 99%