Molecular Plant Pathogen Interactions
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Recent papers in Molecular Plant Pathogen Interactions
This study was conducted to find the incidence of root knot nematode (M. javanica) in winter weeds of tomato at the root knot infested areas of Dargai and Jabban in Malakand division of Khyber Pakhtunkhwa province of Pakistan. For this... more
This study was conducted to find the incidence of root knot nematode (M. javanica) in winter weeds of tomato at the root knot infested areas of Dargai and Jabban in Malakand division of Khyber Pakhtunkhwa province of Pakistan. For this purpose survey was conducted on 20 fields of each region and the fifteen weed plants were checked for galls caused by M. javanica on their roots. Weeds samples from these regions were bagged and labeled properly and brought to the Department of Weed Science, The University of Agriculture, Peshawar Pakistan for identification. The nematode was also identified by perennial pattern. Galls were observed on commonly occurring fifteen weeds. Incidence of M. javanica on Cannabis sativa was at the range of 9.9-11.9%, while it was 33.3% on Digitaria sanguinalis. The highest incidence of M. javanica were recorded on the roots of Fumeria indica (21.05-43.47%). Moreover the incidence of M. javanica on Rumex crispus and Melilotus indica was 22.72% and 22.13% respectively. However no galls (No incidence) of M. javanica were found on Asphodelus tenuifolius. Our finding demonstrates that M. javanica is a damaging pathogen of winter weeds of tomato in Malakand division of Khyber Pakhtunkhwa province of Pakistan.
In animals, heterotrimeric G proteins, comprising Ga, Gb, andGg subunits, are molecular switches whose function tightly depends on Ga and Gbg interaction. Intriguingly, in Arabidopsis (Arabidopsis thaliana), multiple defense responses... more
In animals, heterotrimeric G proteins, comprising Ga, Gb, andGg subunits, are molecular switches whose function tightly depends
on Ga and Gbg interaction. Intriguingly, in Arabidopsis (Arabidopsis thaliana), multiple defense responses involve Gbg, but notGa.
We report here that the Gbg dimer directly partners with extra-large G proteins (XLGs) to mediate plant immunity. Arabidopsis
mutants deficient in XLGs, Gb, and Gg are similarly compromised in several pathogen defense responses, including disease
development and production of reactive oxygen species. Genetic analysis of double, triple, and quadruple mutants confirmed
that XLGs and Gbg functionally interact in the same defense signaling pathways. In addition, mutations in XLG2 suppressed the
seedling lethal and cell death phenotypes of BRASSINOSTEROID INSENSITIVE1-associated receptor kinase1-interacting receptor-like
kinase1 mutants in an identical way as reported for Arabidopsis Gb-deficient mutants. Yeast (Saccharomyces cerevisiae) three-hybrid
and bimolecular fluorescent complementation assays revealed that XLG2 physically interacts with all three possible Gbg dimers at
the plasma membrane. Phylogenetic analysis indicated a close relationship between XLGs and plant Ga subunits, placing the
divergence point at the dawn of land plant evolution. Based on these findings, we conclude that XLGs form functional complexes
with Gbg dimers, although the mechanism of action of these complexes, including activation/deactivation, must be radically
different form the one used by the canonical Ga subunit and are not likely to share the same receptors. Accordingly, XLGs expand
the repertoire of heterotrimeric G proteins in plants and reveal a higher level of diversity in heterotrimeric G protein signaling.
on Ga and Gbg interaction. Intriguingly, in Arabidopsis (Arabidopsis thaliana), multiple defense responses involve Gbg, but notGa.
We report here that the Gbg dimer directly partners with extra-large G proteins (XLGs) to mediate plant immunity. Arabidopsis
mutants deficient in XLGs, Gb, and Gg are similarly compromised in several pathogen defense responses, including disease
development and production of reactive oxygen species. Genetic analysis of double, triple, and quadruple mutants confirmed
that XLGs and Gbg functionally interact in the same defense signaling pathways. In addition, mutations in XLG2 suppressed the
seedling lethal and cell death phenotypes of BRASSINOSTEROID INSENSITIVE1-associated receptor kinase1-interacting receptor-like
kinase1 mutants in an identical way as reported for Arabidopsis Gb-deficient mutants. Yeast (Saccharomyces cerevisiae) three-hybrid
and bimolecular fluorescent complementation assays revealed that XLG2 physically interacts with all three possible Gbg dimers at
the plasma membrane. Phylogenetic analysis indicated a close relationship between XLGs and plant Ga subunits, placing the
divergence point at the dawn of land plant evolution. Based on these findings, we conclude that XLGs form functional complexes
with Gbg dimers, although the mechanism of action of these complexes, including activation/deactivation, must be radically
different form the one used by the canonical Ga subunit and are not likely to share the same receptors. Accordingly, XLGs expand
the repertoire of heterotrimeric G proteins in plants and reveal a higher level of diversity in heterotrimeric G protein signaling.
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