dc.identifier.uri |
http://dx.doi.org/10.15488/5060 |
|
dc.identifier.uri |
https://www.repo.uni-hannover.de/handle/123456789/5104 |
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dc.contributor.author |
Hoyer, Elisabeth
|
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dc.contributor.author |
Knöppel, Julius
|
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dc.contributor.author |
Liebmann, Martina
|
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dc.contributor.author |
Steppert, Michael
|
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dc.contributor.author |
Raiwa, Manuel
|
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dc.contributor.author |
Herczynski, Olivia
|
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dc.contributor.author |
Hanspach, Erik
|
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dc.contributor.author |
Zehner, Susanne
|
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dc.contributor.author |
Göttfert, Michael
|
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dc.contributor.author |
Tsushima, Satoru
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dc.contributor.author |
Fahmy, Karim
|
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dc.contributor.author |
Oertel, Jana
|
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dc.date.accessioned |
2019-07-02T07:58:21Z |
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dc.date.available |
2019-07-02T07:58:21Z |
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dc.date.issued |
2019 |
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dc.identifier.citation |
Hoyer, E.; Knöppel, J.; Liebmann, M.; Steppert, M.; Raiwa, M. et al.: Calcium binding to a disordered domain of a type III-secreted protein from a coral pathogen promotes secondary structure formation and catalytic activity. In: Scientific Reports 9 (2019), Nr. 1, 7115. DOI: https://doi.org/10.1038/s41598-019-42898-0 |
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dc.description.abstract |
Strains of the Gram-negative bacterium Vibrio coralliilyticus cause the bleaching of corals due to decomposition of symbiotic microalgae. The V. coralliilyticus strain ATCC BAA-450 (Vc450) encodes a type III secretion system (T3SS). The gene cluster also encodes a protein (locus tag VIC_001052) with sequence homology to the T3SS-secreted nodulation proteins NopE1 and NopE2 of Bradyrhizobium japonicum (USDA110). VIC_001052 has been shown to undergo auto-cleavage in the presence of Ca 2+ similar to the NopE proteins. We have studied the hitherto unknown secondary structure, Ca 2+ -binding affinity and stoichiometry of the “metal ion-inducible autocleavage” (MIIA) domain of VIC_001052 which does not possess a classical Ca 2+ -binding motif. CD and fluorescence spectroscopy revealed that the MIIA domain is largely intrinsically disordered. Binding of Ca 2+ and other di- and trivalent cations induced secondary structure and hydrophobic packing after partial neutralization of the highly negatively charged MIIA domain. Mass spectrometry and isothermal titration calorimetry showed two Ca 2+ -binding sites which promote structure formation with a total binding enthalpy of −110 kJ mol −1 at a low micromolar K d . Putative binding motifs were identified by sequence similarity to EF-hand domains and their structure analyzed by molecular dynamics simulations. The stoichiometric Ca 2+ -dependent induction of structure correlated with catalytic activity and may provide a “host-sensing” mechanism that is shared among pathogens that use a T3SS for efficient secretion of disordered proteins. |
eng |
dc.language.iso |
eng |
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dc.publisher |
London : Nature Publishing Group |
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dc.relation.ispartofseries |
Scientific Reports 9 (2019), Nr. 1 |
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dc.rights |
CC BY 4.0 Unported |
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dc.rights.uri |
https://creativecommons.org/licenses/by/4.0/ |
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dc.subject |
Calcium |
eng |
dc.subject |
protein |
eng |
dc.subject |
CA2+ |
eng |
dc.subject |
stoichiometry |
eng |
dc.subject.ddc |
500 | Naturwissenschaften
|
ger |
dc.subject.ddc |
600 | Technik
|
ger |
dc.title |
Calcium binding to a disordered domain of a type III-secreted protein from a coral pathogen promotes secondary structure formation and catalytic activity |
eng |
dc.type |
Article |
|
dc.type |
Text |
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dc.relation.issn |
2045-2322 |
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dc.relation.doi |
https://doi.org/10.1038/s41598-019-42898-0 |
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dc.bibliographicCitation.issue |
1 |
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dc.bibliographicCitation.volume |
9 |
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dc.bibliographicCitation.firstPage |
7115 |
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dc.description.version |
publishedVersion |
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tib.accessRights |
frei zug�nglich |
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