<i>Yersinia enterocolitica</i> type III secretion of YopR requires a structure in its mRNA

Blaylock, Bill; Sorg, Joseph A.; Schneewind, Olaf

doi:10.1111/j.1365-2958.2008.06474.x

Cited by 18 publications

(19 citation statements)

References 68 publications

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“…Our data do not support a role for signal peptides in polar localization, but we cannot exclude a role in helical distribution. Localization information may be carried by mRNAs (4,47). Alternatively, B , InlA, InlH, and/or SrtA may shuttle from one place to another by interacting with components of elongase or divisome complexes, or B -dependent PG proteins may be more resistant to proteolysis in the pole region.…”

Section: Discussionmentioning

confidence: 99%

Regulated Shift from Helical to Polar Localization of Listeria monocytogenesCell Wall-Anchored Proteins

et al. 2011

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Many virulence factors of Gram-positive bacterial pathogens are covalently anchored to the peptidoglycan (PG) by sortase enzymes. However, for rod-shaped bacteria little is known about the spatiotemporal organization of these surface proteins in the cell wall. Here we report the three-dimensional (3D) localization of the PG-bound virulence factors InlA, InlH, InlJ, and SvpA in the envelope of Listeria monocytogenes under different growth conditions. We found that all PG-anchored proteins are positioned along the lateral cell wall in nonoverlapping helices. However, these surface proteins can also become localized at the pole and asymmetrically distributed when specific regulatory pathways are activated. InlA and InlJ are enriched at poles when expressed at high levels in exponential-phase bacteria. InlA and InlH, which are B dependent, specifically relocalize to the septal cell wall and subsequently to the new pole in cells entering stationary phase. The accumulation of InlA and InlH in the septal region also occurs when oxidative stress impairs bacterial growth. In contrast, the iron-dependent protein SvpA is present at the old pole and is excluded from the septum and new pole of bacteria grown under low-iron conditions. We conclude that L. monocytogenes rapidly reorganizes the spatial localization of its PG proteins in response to changes in environmental conditions such as nutrient deprivation or other stresses. This dynamic control would distribute virulence factors at specific sites during the infectious process.

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Section: Discussionmentioning

confidence: 99%

Regulated Shift from Helical to Polar Localization of Listeria monocytogenesCell Wall-Anchored Proteins

et al. 2011

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“…Studies from various organisms show numerous silent mutations within the signal sequence have no or little effect on export, implying that the export signal is predominantly encoded in the amino acid sequence [177][178][179]. However, it has also been shown that frameshifted mRNA export sequences can still support the export of substrates and that the mRNA sequence around the start codon plays a role in export ( [180,181], reviewed in [182]), indicating that the effects of mRNA and protein sequence on targeting may be additive.…”

Section: Export Signalsmentioning

confidence: 99%

Type III secretion systems: the bacterial flagellum and the injectisome

Diepold

Armitage

2015

Phil. Trans. R. Soc. B

189

175

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One contribution of 12 to a theme issue 'The bacterial cell envelope'. The flagellum and the injectisome are two of the most complex and fascinating bacterial nanomachines. At their core, they share a type III secretion system (T3SS), a transmembrane export complex that forms the extracellular appendages, the flagellar filament and the injectisome needle. Recent advances, combining structural biology, cryo-electron tomography, molecular genetics, in vivo imaging, bioinformatics and biophysics, have greatly increased our understanding of the T3SS, especially the structure of its transmembrane and cytosolic components, the transcriptional, post-transcriptional and functional regulation and the remarkable adaptivity of the system. This review aims to integrate these new findings into our current knowledge of the evolution, function, regulation and dynamics of the T3SS, and to highlight commonalities and differences between the two systems, as well as their potential applications.

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“…This could also explain the slight reduction in YopD I3,5N secretion compared to YopD FrameϪ1, I3,4N secretion; whereas the proportions of serine, threonine, and proline residues are consistent between the two, the former protein has a more restricted distribution of hydrophobic amino acids (see Table 2). It is also worth keeping in mind that N-terminal-mediated substrate secretion can be influenced by the sequence composition further downstream; secretion of the T3S of YopR (also termed YscH) by Yersinia requires a distinct mRNA motif nearer the C terminus that cooperates with the typical N-terminal amino acid signal (9). The presence of such an internal secondary mRNA sequence in YopD has not been investigated.…”

Section: Discussionmentioning

confidence: 99%

Impact of the N-Terminal Secretor Domain on YopD Translocator Function in Yersinia pseudotuberculosis Type III Secretion

et al. 2011

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Type III secretion systems (T3SSs) secrete needle components, pore-forming translocators, and the translocated effectors. In part, effector recognition by a T3SS involves their N-terminal amino acids and their 5 mRNA. To investigate whether similar molecular constraints influence translocator secretion, we scrutinized this region within YopD from Yersinia pseudotuberculosis. Mutations in the 5 end of yopD that resulted in specific disruption of the mRNA sequence did not affect YopD secretion. On the other hand, a few mutations affecting the protein sequence reduced secretion. Translational reporter fusions identified the first five codons as a minimal N-terminal secretion signal and also indicated that the YopD N terminus might be important for yopD translation control. Hybrid proteins in which the N terminus of YopD was exchanged with the equivalent region of the YopE effector or the YopB translocator were also constructed. While the in vitro secretion profile was unaltered, these modified bacteria were all compromised with respect to T3SS activity in the presence of immune cells. Thus, the YopD N terminus does harbor a secretion signal that may also incorporate mechanisms of yopD translation control. This signal tolerates a high degree of variation while still maintaining secretion competence suggestive of inherent structural peculiarities that make it distinct from secretion signals of other T3SS substrates.

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Yersinia enterocolitica type III secretion of YopR requires a structure in its mRNA

Cited by 18 publications

References 68 publications

Regulated Shift from Helical to Polar Localization of Listeria monocytogenesCell Wall-Anchored Proteins

Regulated Shift from Helical to Polar Localization of Listeria monocytogenesCell Wall-Anchored Proteins

Type III secretion systems: the bacterial flagellum and the injectisome

Impact of the N-Terminal Secretor Domain on YopD Translocator Function in Yersinia pseudotuberculosis Type III Secretion

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