Dual client binding sites in the ATP-independent chaperone SurA
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F24%3A43908806" target="_blank" >RIV/60076658:12310/24:43908806 - isvavai.cz</a>
Result on the web
<a href="https://www.nature.com/articles/s41467-024-52021-1" target="_blank" >https://www.nature.com/articles/s41467-024-52021-1</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41467-024-52021-1" target="_blank" >10.1038/s41467-024-52021-1</a>
Alternative languages
Result language
angličtina
Original language name
Dual client binding sites in the ATP-independent chaperone SurA
Original language description
The ATP-independent chaperone SurA protects unfolded outer membrane proteins (OMPs) from aggregation in the periplasm of Gram-negative bacteria, and delivers them to the beta-barrel assembly machinery (BAM) for folding into the outer membrane (OM). Precisely how SurA recognises and binds its different OMP clients remains unclear. Escherichia coli SurA comprises three domains: a core and two PPIase domains (P1 and P2). Here, by combining methyl-TROSY NMR, single-molecule F & ouml;rster resonance energy transfer (smFRET), and bioinformatics analyses we show that SurA client binding is mediated by two binding hotspots in the core and P1 domains. These interactions are driven by aromatic-rich motifs in the client proteins, leading to SurA core/P1 domain rearrangements and expansion of clients from collapsed, non-native states. We demonstrate that the core domain is key to OMP expansion by SurA, and uncover a role for SurA PPIase domains in limiting the extent of expansion. The results reveal insights into SurA-OMP recognition and the mechanism of activation for an ATP-independent chaperone, and suggest a route to targeting the functions of a chaperone key to bacterial virulence and OM integrity. Dual binding sites are identified in the outer membrane chaperone SurA, providing substrate recognition and mechanistic insights into this ATP-independent chaperone.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10610 - Biophysics
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature Communications
ISSN
2041-1723
e-ISSN
2041-1723
Volume of the periodical
15
Issue of the periodical within the volume
1
Country of publishing house
DE - GERMANY
Number of pages
16
Pages from-to
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UT code for WoS article
001335565900001
EID of the result in the Scopus database
2-s2.0-85204024958