Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 45, Pages -Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.395129
Keywords
-
Categories
Funding
- Biotechnology and Biological Sciences Research Council (BBSRC)
- Natural Environmental Research Council (NERC)
- University of Aberdeen
- University of Dundee
- Scottish Government Rural and Environmental Science Analytical Services Division (RESAS)
- Royal Society
- BBSRC [BB/G015244/1, BB/E007120/1] Funding Source: UKRI
- NERC [NE/J00460X/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E007120/1, BB/G015244/1] Funding Source: researchfish
- Natural Environment Research Council [NE/J00460X/1] Funding Source: researchfish
Ask authors/readers for more resources
The mechanism of translocation of RxLR effectors from plant pathogenic oomycetes into the cytoplasm of their host is currently the object of intense research activity and debate. Here, we report the biochemical and thermodynamic characterization of the Phytophthora infestans effector AVR3a in vitro. We show that the amino acids surrounding the RxLR leader mediate homodimerization of the protein. Dimerization was considerably attenuated by a localized mutation within the RxLR motif that was previously described to prevent translocation of the protein into host. Importantly, we confirm that the reported phospholipid-binding properties of AVR3a are mediated by its C-terminal effector domain, not its RxLR leader. However, we show that the observed phospholipid interaction is attributable to a weak association with denatured protein molecules and is therefore most likely physiologically irrelevant.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available