Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein

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Weise, Christoph FUmeå universitet,Kemiska institutionen (author)

Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein

Article/chapterEnglish2014

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Cell Press,2014
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LIBRIS-ID:oai:DiVA.org:umu-95192
https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-95192URI
https://doi.org/10.1016/j.bpj.2014.09.005DOI

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Language:English
Summary in:English

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Subject category:art swepub-publicationtype

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The inner membrane of Gram-negative bacteria is negatively charged, rendering positively charged cytoplasmic proteins in close proximity likely candidates for protein-membrane interactions. YscU is a Yersinia pseudotuberculosis type III secretion system protein crucial for bacterial pathogenesis. The protein contains a highly conserved positively charged linker sequence that separates membrane-spanning and cytoplasmic (YscUC) domains. Although disordered in solution, inspection of the primary sequence of the linker reveals that positively charged residues are separated with a typical helical periodicity. Here, we demonstrate that the linker sequence of YscU undergoes a largely electrostatically driven coil-to-helix transition upon binding to negatively charged membrane interfaces. Using membrane-mimicking sodium dodecyl sulfate micelles, an NMR derived structural model reveals the induction of three helical segments in the linker. The overall linker placement in sodium dodecyl sulfate micelles was identified by NMR experiments including paramagnetic relaxation enhancements. Partitioning of individual residues agrees with their hydrophobicity and supports an interfacial positioning of the helices. Replacement of positively charged linker residues with alanine resulted in YscUC variants displaying attenuated membrane-binding affinities, suggesting that the membrane interaction depends on positive charges within the linker. In vivo experiments with bacteria expressing these YscU replacements resulted in phenotypes displaying significantly reduced effector protein secretion levels. Taken together, our data identify a previously unknown membrane-interacting surface of YscUC that, when perturbed by mutations, disrupts the function of the pathogenic machinery in Yersinia.

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NATURVETENSKAP Biologi Biofysik hsv//swe
NATURAL SCIENCES Biological Sciences Biophysics hsv//eng

Added entries (persons, corporate bodies, meetings, titles ...)

Login, Frédéric HUmeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR)(Swepub:umu)frlo0006 (author)
Ho, OanhUmeå universitet,Kemiska institutionen(Swepub:umu)hooa0003 (author)
Gröbner, GerhardUmeå universitet,Kemiska institutionen(Swepub:umu)gegr0001 (author)
Wolf-Watz, HansUmeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR)(Swepub:umu)hawo0001 (author)
Wolf-Watz, MagnusUmeå universitet,Kemiska institutionen(Swepub:umu)maswoz04 (author)
Umeå universitetKemiska institutionen (creator_code:org_t)

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In:Biophysical Journal: Cell Press107:8, s. 1950-19610006-34951542-0086

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NATURAL SCIENCES: NATURAL SCIENCES; and Biological Scien ...; and Biophysics

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By the university: Umeå University

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