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Molecular dialog between two ingenious opponents-plants and pathogenic bacteria
Published on 2014-02-242356 Views
Pseudomonas syringae pv. phaseolicola is the causative agent of halo blight in Phaseolus vulgaris L., the common bean. Similar to other pathogenic Gram-negative bacteria, P. syringae delivers type III
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Presentation
Molecular dialog between two ingenious opponents-plants and pathogenic bacteria00:00
PAMP Triggered Immunity (PTI)00:06
Zigzag model01:10
Transmission electron micrographs of epidermal cells of tobacco leaves infected with Pseudomonas syringae02:38
Structure of Type Three Secretion System of Pseudomonas syringae pv. tomato DC300002:54
Structure of Type Three Secretion System Salmonella subsp. enterica ser. typhimurium03:01
HopQ1 plays a role in determining the host range of Pseudomonas syringae03:30
HopQ1 model (i-tasser)04:26
HopQ1 - 105:06
HopQ1 co-purifies with 14-3-3 proteins from N. benthamiana05:36
Mass spectrometry analysis06:01
The 14-3-3 binding site is conserved in HopQ1, the TTSS effector from Pseudomonas syringae, and XopQ, its xenolog from Xanthomonas spp.06:03
Kinase activity capable of phosphorylating HopQ1 is ubiquitously conserved in plants06:16
The predicted 14-3-3–binding motif of HopQ1 is phosphorylated by plant kinases06:36
Serine 51 plays a critical role in the phosphorylation of HopQ107:00
FRET-FLIM analysis showing that HopQ1 S51 is critical for 14-3-3a binding07:26
HopQ1 binds to 14-3-3a in phosphorylation dependent manner08:20
Interaction with 14-3-3s can affect various aspects of partner proteins09:19
Subcellular localization of HopQ1 variants09:51
Co-expression of 14-3-3a and HopQ1 affects nuclear-cytoplasmic partitioning of the binding partners10:33
Interaction with 14-3-3 proteins affects HopQ1 stability in plants10:53
R18 dramatically reduces stability of in vitro assembled complex of HopQ1-Flag and 14-3-3a-Strep incubated with bean crude protein extract11:24
Assesment of virulence properties of HopQ1 effector mutated to eliminate 14-3-3 binding12:32
Small Angle X-ray Scattering (SAXS) and X-ray crystallography14:59
Biological Small Angle X-ray Scattering15:55
SAXS16:13
Multi Angle Light Scattering17:00
HopQ1-14-3-3a complex - 117:36
HopQ1-14-3-3a complex - 217:53
HopQ1-14-3-3a complex - 318:12
HopQ1 forms oligomers18:40
Disulphide-linked oligomers of HopQ119:00
Chelation of calcium ions induces HopQ1 dimer formation in the presence of DTT (gel filtration)19:48
HopQ1 - 220:26
Mutation in calcium binding motif leads to dimer formation20:47
Chelation of calcium ions induces HopQ1 dimer formation in the presence of DTT (SAXS)21:07
Structure of HopQ1 dimer (SAXS analysis)21:37
RihA, NH from Escherichia coli, forms tetramers21:47
RihA forms tetramers in the presence of EDTA22:16
Conclusions22:42
COST23:20
Acknowledgments23:55