Author
Listed:
- Thomas Jank
(Institute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University Freiburg)
- Stephanie Eckerle
(Institute Biology I, Faculty of Biology, Albert-Ludwigs-University Freiburg)
- Marcus Steinemann
(Institute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University Freiburg)
- Christoph Trillhaase
(Institute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University Freiburg)
- Marianne Schimpl
(MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee)
- Sebastian Wiese
(Center for Biological Systems Analysis, Albert-Ludwigs-University Freiburg)
- Daan M. F. van Aalten
(MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee)
- Wolfgang Driever
(Institute Biology I, Faculty of Biology, Albert-Ludwigs-University Freiburg
Centre for Biological Signalling Studies (BIOSS), Albert-Ludwigs-University Freiburg)
- Klaus Aktories
(Institute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs-University Freiburg
Centre for Biological Signalling Studies (BIOSS), Albert-Ludwigs-University Freiburg)
Abstract
Yersinia species cause zoonotic infections, including enterocolitis and plague. Here we studied Yersinia ruckeri antifeeding prophage 18 (Afp18), the toxin component of the phage tail-derived protein translocation system Afp, which causes enteric redmouth disease in salmonid fish species. Here we show that microinjection of the glycosyltransferase domain Afp18G into zebrafish embryos blocks cytokinesis, actin-dependent motility and cell blebbing, eventually abrogating gastrulation. In zebrafish ZF4 cells, Afp18G depolymerizes actin stress fibres by mono-O-GlcNAcylation of RhoA at tyrosine-34; thereby Afp18G inhibits RhoA activation by guanine nucleotide exchange factors, and blocks RhoA, but not Rac and Cdc42 downstream signalling. The crystal structure of tyrosine-GlcNAcylated RhoA reveals an open conformation of the effector loop distinct from recently described structures of GDP- or GTP-bound RhoA. Unravelling of the molecular mechanism of the toxin component Afp18 as glycosyltransferase opens new perspectives in studies of phage tail-derived protein translocation systems, which are preserved from archaea to human pathogenic prokaryotes.
Suggested Citation
Thomas Jank & Stephanie Eckerle & Marcus Steinemann & Christoph Trillhaase & Marianne Schimpl & Sebastian Wiese & Daan M. F. van Aalten & Wolfgang Driever & Klaus Aktories, 2015.
"Tyrosine glycosylation of Rho by Yersinia toxin impairs blastomere cell behaviour in zebrafish embryos,"
Nature Communications, Nature, vol. 6(1), pages 1-16, November.
Handle:
RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8807
DOI: 10.1038/ncomms8807
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