Structure of Spa15, a type III secretion chaperone from <i>Shigella flexneri</i> with broad specificity

Eerde, André van; Hamiaux, Cyril; Pérez, Javier; Parsot, Claude; Dijkstra, Bauke W.

doi:10.1038/sj.embor.7400144

Cited by 51 publications

(57 citation statements)

References 26 publications

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“…2C) (16,17) displays that ␣-helices H1 and H3 as well as ␤-strands S1-S5 colocalize very nicely but do so in only one subunit because of considerable variation of subunit tilting. The latter phenomenon is most pronounced in the structure of S. flexneri Spa15 (19). The Spa15 monomer, however, exhibited the same overall fold as class IA chaperones.…”

Section: Discussionmentioning

confidence: 87%

“…The SycH fold also resembles that of the aforementioned chaperones (16); however, its biologically relevant oligomerization state is not unambiguously clear (21). The fold of the class IB chaperone Spa15 is very similar to that of class IA chaperones; dimer formation, however, is different, with the subunits rotated relative to each other (19). The crystal structure of the flagellar secretion chaperone FliS (class III) reveals a fold distinct from that of pathogenicity-related TTSS secretion chaperones (20).…”

mentioning

confidence: 94%

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Crystal Structure of the Yersinia enterocolitica Type III Secretion Chaperone SycT

Locher

Lehnert

Krauss

et al. 2005

Journal of Biological Chemistry

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Several Gram-negative pathogens deploy type III secretion systems (TTSSs) as molecular syringes to inject effector proteins into host cells. Prior to secretion, some of these effectors are accompanied by specific type III secretion chaperones. The Yersinia enterocolitica TTSS chaperone SycT escorts the effector YopT, a cysteine protease that inactivates the small GTPase RhoA of targeted host cells. We solved the crystal structure of SycT at 2.5 Å resolution. Despite limited sequence similarity among TTSS chaperones, the SycT structure revealed a global fold similar to that exhibited by other structurally solved TTSS chaperones. The dimerization domain of SycT, however, differed from that of all other known TTSS chaperone structures. Thus, the dimerization domain of TTSS chaperones does not likely serve as a general recognition pattern for downstream processing of effector/chaperone complexes. Yersinia Yop effectors are bound to their specific Syc chaperones close to the Yop N termini, distinct from their catalytic domains. Here, we showed that the catalytically inactive YopT C139S is reduced in its ability to bind SycT, suggesting an ancillary interaction between YopT and SycT. This interaction could maintain the protease inactive prior to secretion or could influence the secretion competence and folding of YopT.

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Section: Discussionmentioning

confidence: 87%

mentioning

confidence: 94%

Crystal Structure of the Yersinia enterocolitica Type III Secretion Chaperone SycT

Locher

Lehnert

Krauss

et al. 2005

Journal of Biological Chemistry

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“…Considering that two InvB can bind per SipA (26,27), we estimated that SipA can reach local concentrations sufficient for remodeling the host cell actin cytoskeleton in vitro and in vivo within 16-25 sec after docking (5,7,18,28). SopE is injected with kinetics similar to those of SipA, but it does not accumulate in foci (Fig.…”

Section: Resultsmentioning

confidence: 99%

Real-time imaging of type III secretion: Salmonella SipA injection into host cells

Schlumberger¹,

Müller²,

Ehrbar³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

179

200

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Many pathogenic and symbiotic Gram-negative bacteria employ type III secretion systems to inject ''effector'' proteins into eukaryotic host cells. These effectors manipulate signaling pathways to initiate symbiosis or disease. By using time-lapse microscopy, we have imaged delivery of the Salmonella type III effector protein SipA͞SspA into animal cells in real time. SipA delivery mostly began 10 -90 sec after docking and proceeded for 100 -600 sec until the bacterial SipA pool (6 ؎ 3 ؋ 10 3 molecules) was exhausted. Similar observations were made for the effector protein SopE. This visualization of type III secretion in real time explains the efficiency of host cell manipulation by means of this virulence system. effector protein ͉ time-lapse microscopy

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“…However, some examples of chaperones binding to multiple substrates have been reported (van Eerde et al, 2004), so promiscuity in the chaperones of effectors from Er. amylovora would not be implausible.…”

Section: Cbds Of Dspa/ementioning

confidence: 99%

Secretion and translocation signals and DspB/F-binding domains in the type III effector DspA/E of Erwinia amylovora

Carpenter

Hayes

et al. 2010

Microbiology

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DspA/E is a type III effector of Erwinia amylovora, the bacterial pathogen that causes fire blight disease in roseaceous plants. This effector is indispensable for disease development, and it is translocated into plant cells. A DspA/E-specific chaperone, DspB/F, is necessary for DspA/E secretion and possibly for its translocation. In this work, DspB/F-binding sites and secretion and translocation signals in the DspA/E protein were determined. Based on yeast two-hybrid assays, DspB/F was found to bind DspA/E within the first 210 amino acids of the protein. Surprisingly, both DspB/F and OrfA, the putative chaperone of Eop1, also interacted with the C-terminal 1059 amino acids of DspA/E; this suggests another chaperone-binding site. Secretion and translocation assays using serial N-terminal lengths of DspA/E fused with the active form of AvrRpt2 revealed that at least the first 109 amino acids, including the first N-terminal chaperone-binding motif and DspB/F, were required for efficient translocation of DspA/E, although the first 35 amino acids were sufficient for its secretion and the presence of DspB/F was not required. These results indicate that secretion and translocation signals are present in the N terminus of DspA/E, and that at least one DspB/F-binding motif is required for efficient translocation into plant cells.

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Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity

Cited by 51 publications

References 26 publications

Crystal Structure of the Yersinia enterocolitica Type III Secretion Chaperone SycT

Crystal Structure of the Yersinia enterocolitica Type III Secretion Chaperone SycT

Real-time imaging of type III secretion: Salmonella SipA injection into host cells

Secretion and translocation signals and DspB/F-binding domains in the type III effector DspA/E of Erwinia amylovora

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