Uncovering genomic differences in human pathogenic<i>Yersinia enterocolitica</i>

Golubov, Andrey; Heesemann, J.; Rakin, Alexander

doi:10.1016/s0928-8244(03)00182-2

Cited by 15 publications

(12 citation statements)

References 34 publications

(46 reference statements)

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“…2). We have found this pair of crystallin paralogues in the genome of Y. pseudotuberculosis and Y. enterocolitica (37) with minor variations and also in other strains of Y. pestis, namely strain 91001 (38) and Kurdistan Iran Man (KIM) (39). We have also identified a hypothetical protein (GenBank TM accession number CAG22738, locus tag PBPRB0866) having homology to Yersinia crystallin with two crystallin domains, in the genome of Photobacterium profundum, 2 a marine bacterium living at high pressure and low temperature (Fig.…”

Section: Resultsmentioning

confidence: 98%

“…We suggest that, by similarity with other crystallins, Yersinia crystallin might be protecting the bacterium during adverse conditions, because domain D1 is stabilized by calcium, and D2 can act as a calcium buffer. On the basis of genomic differences between virulent and nonvirulent strains, Golubov et al (37) reported the presence of Yersinia crystallin and its paralogue in Y. enterocolitica with possible impact on virulence. Therefore, a possible role of Yersinia crystallin in virulence cannot be ruled out completely.…”

Section: Table II Deconvulation Of Far Uv Cd Spectra Of D1 and D2mentioning

confidence: 99%

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Calcium-binding Crystallins from Yersinia pestis

Jobby¹,

Sharma

2005

Journal of Biological Chemistry

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␤␥-Crystallin is a superfamily with diverse members from vertebrate lens to microbes. However, not many members have been identified and studied. Here, we report the identification of a putative exported protein from Yersinia pestis as a member of the ␤␥-crystallin superfamily. Even though calcium has been known to play an important role in the physiology and virulence of the Yersinia genus, calcium-binding proteins have not yet been identified. We have studied the calcium-binding properties of two of the three crystallin domains present in this putative exported protein designated "Yersinia crystallin." These two domains (D1 and D2) have unique AA and BB types of arrangement of their Greek key motifs unlike the domains of other members of the ␤␥-crystallin superfamily, which are either AB or BA types. These domains bind two calcium ions with low and high affinity-binding sites. We showed their calcium-binding properties using various probes for calcium and the effect of calcium on their secondary and tertiary structures. Although both domains bind calcium, D1 underwent drastic changes in secondary and tertiary structure and hydrodynamic volume upon calcium binding. Domain D1, which is intrinsically unstructured in the apo form, requires calcium for the typical ␤␥-crystallin fold. Calcium exerted an extrinsic stabilization effect on domain D1 but not on D2, which is also largely unstructured. We suggest that this protein might be involved in calcium-dependent processes, such as stress response or physiology in the Yersinia genus, similar to its microbial relatives and mammalian lens crystallins.

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Section: Resultsmentioning

confidence: 98%

Section: Table II Deconvulation Of Far Uv Cd Spectra Of D1 and D2mentioning

confidence: 99%

Calcium-binding Crystallins from Yersinia pestis

Jobby¹,

Sharma

2005

Journal of Biological Chemistry

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“…This system resembles the Ssa T3SS of Salmonella enterica [39]. It has also been reported that this locus is present in some Y. enterocolitica serotype O:3 strains [40]. To date, no clear link between this T3SS and virulence has been established.…”

Section: New Yersinia Effectors Yet To Be Discoveredmentioning

confidence: 94%

Translocated effectors of Yersinia

Matsumoto

Young

2009

Current Opinion in Microbiology

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SummaryCurrently, all known translocated effectors of Yersinia are delivered into host cells by type III secretion systems (T3SSs). Pathogenic Yersinia maintain the plasmid-encoded Ysc T3SS for the specific delivery of the well-studied Yop effectors. New horizons for effector biology have opened with the discovery of the Ysps of Y. enterocolitica Biovar 1B, which are translocated into host cells by the chromosome-endoded Ysa T3SS. The reported arsenal of effectors is likely to expand since genomic analysis has revealed gene-clusters in some Yersinia that code for other T3SSs. These efforts also revealed possible type VI secretion (T6S) systems, which may indicate translocation of effectors occurs by multiple mechanisms.

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“…Within the superfamily, there exists a stability gradient across the domains and differences in the extent of gain in stability upon Ca 2ϩ binding from very low (in Vibrillin) to very high (in Centillin) (Table 1) (52,84). As noted in Y. pestis, ␤␥ domain-containing proteins are differentially expressed in Ca 2ϩ -depleted avirulent strains (85,86) and are unstructured in apo form (38), raising the prospective of their role in virulence via low calcium response. It is clear that the ␤␥-crystallin domain is widely spread.…”

Section: ؉ Binding and Domain Stabilizationmentioning

confidence: 99%

Ca2+-binding Motif of βγ-Crystallins

Srivastava¹,

Mishra

Krishnan³

et al. 2014

Journal of Biological Chemistry

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␤␥-Crystallin-type double clamp (N/D)(N/D)XX(S/T)S motif is an established but sparsely investigated motif for Ca2؉ binding. A ␤␥-crystallin domain is formed of two Greek key motifs, accommodating two Ca 2؉ -binding sites. ␤␥-Crystallins make a separate class of Ca 2؉ -binding proteins (CaBP), apparently a major group of CaBP in bacteria. Paralleling the diversity in ␤␥-crystallin domains, these motifs also show great diversity, both in structure and in function. Although the expression of some of them has been associated with stress, virulence, and adhesion, the functional implications of Ca 2؉ binding to ␤␥-crystallins in mediating biological processes are yet to be elucidated.

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Uncovering genomic differences in human pathogenicYersinia enterocolitica

Cited by 15 publications

References 34 publications

Calcium-binding Crystallins from Yersinia pestis

Calcium-binding Crystallins from Yersinia pestis

Translocated effectors of Yersinia

Ca2+-binding Motif of βγ-Crystallins

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