A polymorphic helix of a Salmonella needle protein relays
signals defining distinct steps in type III secretion

J 2019

A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion

GUO, E.Z., D.C. DESROSIERS, Jan ZÁLEŠÁK, J. TOLCHARD, M. BERBON et. al.

Základní údaje

Originální název

A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion

Autoři

GUO, E.Z., D.C. DESROSIERS, Jan ZÁLEŠÁK, J. TOLCHARD, M. BERBON, B. HABENSTEIN, T. MARLOVITS, A. LOQUET a J.E. GALAN

Vydání

PLoS Biology, USA, PUBLIC LIBRARY SCIENCE, 2019, 1544-9173

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 7.076

Organizační jednotka

Přírodovědecká fakulta

DOI

http://dx.doi.org/10.1371/journal.pbio.3000351

UT WoS

000478922100013

Změněno: 21. 4. 2020 14:43, Mgr. Marie Šípková, DiS.

Anotace

V originále

Type III protein-secretion machines are essential for the interactions of many pathogenic or symbiotic bacterial species with their respective eukaryotic hosts. The core component of these machines is the injectisome, a multiprotein complex that mediates the selection of substrates, their passage through the bacterial envelope, and ultimately their delivery into eukaryotic target cells. The injectisome is composed of a large cytoplasmic complex or sorting platform, a multiring base embedded in the bacterial envelope, and a needle-like filament that protrudes several nanometers from the bacterial surface and is capped at its distal end by the tip complex. A characteristic feature of these machines is that their activity is stimulated by contact with target host cells. The sensing of target cells, thought to be mediated by the distal tip of the needle filament, generates an activating signal that must be transduced to the secretion machine by the needle filament. Here, through a multidisciplinary approach, including solid-state NMR (SSNMR) and cryo electron microscopy (cryo-EM) analyses, we have identified critical residues of the needle filament protein of a Salmonella Typhimurium type III secretion system that are involved in the regulation of the activity of the secretion machine. We found that mutations in the needle filament protein result in various specific phenotypes associated with different steps in the type III secretion process. More specifically, these studies reveal an important role for a polymorphic helix of the needle filament protein and the residues that line the lumen of its central channel in the control of type III secretion.

Citovat

GUO, E.Z., D.C. DESROSIERS, Jan ZÁLEŠÁK, J. TOLCHARD, M. BERBON, B. HABENSTEIN, T. MARLOVITS, A. LOQUET a J.E. GALAN. A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion. PLoS Biology. USA: PUBLIC LIBRARY SCIENCE, 2019, roč. 17, č. 7, 33 s. ISSN 1544-9173. Dostupné z: https://dx.doi.org/10.1371/journal.pbio.3000351.

@article{1647979,
   author = {Guo, E.Z. and Desrosiers, D.C. and Zálešák, Jan and Tolchard, J. and Berbon, M. and Habenstein, B. and Marlovits, T. and Loquet, A. and Galan, J.E.},
   article_location = {USA},
   article_number = {7},
   doi = {http://dx.doi.org/10.1371/journal.pbio.3000351},
   language = {eng},
   issn = {1544-9173},
   journal = {PLoS Biology},
   note = {Žádný z autorů nemá afiliaci pro MU.},
   title = {A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion},
   volume = {17},
   year = {2019}
}

TY  - JOUR
ID  - 1647979
AU  - Guo, E.Z. - Desrosiers, D.C. - Zálešák, Jan - Tolchard, J. - Berbon, M. - Habenstein, B. - Marlovits, T. - Loquet, A. - Galan, J.E.
PY  - 2019
TI  - A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion
JF  - PLoS Biology
VL  - 17
IS  - 7
PB  - PUBLIC LIBRARY SCIENCE
SN  - 15449173
N1  - Žádný z autorů nemá afiliaci pro MU.
N2  - Type III protein-secretion machines are essential for the interactions of many pathogenic or symbiotic bacterial species with their respective eukaryotic hosts. The core component of these machines is the injectisome, a multiprotein complex that mediates the selection of substrates, their passage through the bacterial envelope, and ultimately their delivery into eukaryotic target cells. The injectisome is composed of a large cytoplasmic complex or sorting platform, a multiring base embedded in the bacterial envelope, and a needle-like filament that protrudes several nanometers from the bacterial surface and is capped at its distal end by the tip complex. A characteristic feature of these machines is that their activity is stimulated by contact with target host cells. The sensing of target cells, thought to be mediated by the distal tip of the needle filament, generates an activating signal that must be transduced to the secretion machine by the needle filament. Here, through a multidisciplinary approach, including solid-state NMR (SSNMR) and cryo electron microscopy (cryo-EM) analyses, we have identified critical residues of the needle filament protein of a Salmonella Typhimurium type III secretion system that are involved in the regulation of the activity of the secretion machine. We found that mutations in the needle filament protein result in various specific phenotypes associated with different steps in the type III secretion process. More specifically, these studies reveal an important role for a polymorphic helix of the needle filament protein and the residues that line the lumen of its central channel in the control of type III secretion.
ER  -

GUO, E.Z., D.C. DESROSIERS, Jan ZÁLEŠÁK, J. TOLCHARD, M. BERBON, B. HABENSTEIN, T. MARLOVITS, A. LOQUET a J.E. GALAN. A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion. \textit{PLoS Biology}. USA: PUBLIC LIBRARY SCIENCE, 2019, roč.~17, č.~7, 33 s. ISSN~1544-9173. Dostupné z: https://dx.doi.org/10.1371/journal.pbio.3000351.

Podrobný výpis o publikaci