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Molecular dialog between two ingenious opponents-plants and pathogenic bacteria
Published on Feb 24, 20142335 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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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
Disulphide-linked oligomers of HopQ119:28
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