Yersinia pestis YopD 150–287 fragment is partially unfolded in the native state

Raab, Ronald W.; Świętnicki, Wiesław

doi:10.1016/j.pep.2007.11.001

Cited by 8 publications

(9 citation statements)

References 38 publications

(44 reference statements)

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“…A soluble internal 150 -287-residue YopD polypeptide has been found to exist stably in an unfolded state (31). This is comparable with the behavior of the PopD N-terminal region, which exists in a loosely folded, highly flexible, molten, globule state (32).…”

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confidence: 70%

“…Evidence also indicates that EspB from enteropathogenic Escherichia coli and IpaC from Shigella flexneri both assume a partially folded state with a significant degree of disordered structure (33,34). All of these structural characteristics may confer several benefits to this protein family; limiting the need for unfolding may promote their efficient secretion and/or pore formation into biological membranes or increase the potential surface area to facilitate physical contacts with multiple protein interaction partners (31)(32)(33)(34).…”

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confidence: 99%

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YopD Self-assembly and Binding to LcrV Facilitate Type III Secretion Activity by Yersinia pseudotuberculosis

Costa

Edqvist

Bröms

et al. 2010

Journal of Biological Chemistry

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YopD-like translocator proteins encoded by several Gramnegative bacteria are important for type III secretion-dependent delivery of anti-host effectors into eukaryotic cells. This probably depends on their ability to form pores in the infected cell plasma membrane, through which effectors may gain access to the cell interior. In addition, Yersinia YopD is a negative regulator essential for the control of effector synthesis and secretion. As a prerequisite for this functional duality, YopD may need to establish molecular interactions with other key T3S components. A putative coiled-coil domain and an ␣-helical amphipathic domain, both situated in the YopD C terminus, may represent key protein-protein interaction domains. Therefore, residues within the YopD C terminus were systematically mutagenized. All 68 mutant bacteria were first screened in a variety of assays designed to identify individual residues essential for YopD function, possibly by providing the interaction interface for the docking of other T3S proteins. Mirroring the effect of a full-length yopD gene deletion, five mutant bacteria were defective for both yop regulatory control and effector delivery. Interestingly, all mutations clustered to hydrophobic amino acids of the amphipathic domain. Also situated within this domain, two additional mutants rendered YopD primarily defective in the control of Yop synthesis and secretion. Significantly, protein-protein interaction studies revealed that functionally compromised YopD variants were also defective in self-oligomerization and in the ability to engage another translocator protein, LcrV. Thus, the YopD amphipathic domain facilitates the formation of YopD/YopD and YopD/LcrV interactions, two critical events in the type III secretion process.

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confidence: 70%

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confidence: 99%

YopD Self-assembly and Binding to LcrV Facilitate Type III Secretion Activity by Yersinia pseudotuberculosis

Costa

Edqvist

Bröms

et al. 2010

Journal of Biological Chemistry

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“…The translocator proteins like PopB, PopD are shown to have molten globule conformation at all pH [14, 35, data to be published]. Also, a fragment of YopD(150-287) from Y. pestis is partially unfolded in the native state [34]. Therefore, in absence of its chaperone SycB, YspC can be highly soluble and maintain a stable structure.…”

Section: Discussionmentioning

confidence: 99%

“…3-D experimental structures are available for peptides of translocators bound to class II chaperones [23,25]. Also, fragments of translocators have been structurally elucidated by X-ray crystallography and NMR spectroscopy [1,34,38], but structures of full length translocators and translocator-chaperone complexes are still not available. From the FRET efficiency, a prediction can be made that YspC shows a much compact structure compared to SycB.…”

Section: Discussionmentioning

confidence: 99%

YspC: A Unique Translocator Exhibits Structural Alteration in the Complex form with Chaperone SycB

2012

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YspC is an annotated translocator of Yersinia secretion apparatus-Yersinia secretion protein type three secretion system of Yersinia enterocolitica, it forms an 1:1 complex with its cognate chaperone SycB. Unlike other translocators, YspC is highly soluble inspite of having a transmembrane region. Size exclusion chromatography shows that YspC exists predominantly in a monomeric form. Multiple sequence alignment and ConSurf (a web based bioinformatic tool) analysis confirm its significant deviation from the closest class of minor translocators. YspC also possesses a tertiary structure signal seen from near UV CD, further confirming its unique nature amongst the groups of translocators. Far UV CD depicts that YspC is predominantly an α-helical protein; however, its secondary structure alters in the YspC-SycB complex. Thermal denaturation curve predicts a cooperative melting behaviour for YspC which is altered in the YspC-SycB complex. Furthermore, trypsinolysis data confirms a different digestion pattern for YspC in isolation, when compared to the complex form with SycB. From the Forsters resonance energy transfer analysis, it can be predicted that the two tetratricopeptide repeat regions of SycB are masked while it forms a complex with YspC and this is further confirmed by the interaction studies of YspC with two truncated forms of SycB. YspC interacted with ∆SycB₁₋₁₁₄ and ∆SycB₃₆₋₁₁₄ (possessing only the two TPR regions). However, the complexes formed between YspC and truncated forms of SycB have altered physiological states.

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“…It is highly soluble and very stable and possesses rigid tertiary structure. Till now, only the structures of small peptides or fragments of translocator proteins are available [18,26,27,28]. Therefore, it would Interestingly, these helices do not occur in a sequential manner.…”

Section: Homology Model Of Yspc Shows An Elongated Y-shaped Structurementioning

confidence: 99%

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Yersinia pestis YopD 150–287 fragment is partially unfolded in the native state

Cited by 8 publications

References 38 publications

YopD Self-assembly and Binding to LcrV Facilitate Type III Secretion Activity by Yersinia pseudotuberculosis

YopD Self-assembly and Binding to LcrV Facilitate Type III Secretion Activity by Yersinia pseudotuberculosis

YspC: A Unique Translocator Exhibits Structural Alteration in the Complex form with Chaperone SycB

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