Interactions
Follow
Find
62 views | +0 today
Your new post is loading...
Your new post is loading...
Scooped by Gautam Shirsekar
Scoop.it!

PLOS Pathogens: The Plant Actin Cytoskeleton Responds to Signals from Microbe-Associated Molecular Patterns

PLOS Pathogens: The Plant Actin Cytoskeleton Responds to Signals from Microbe-Associated Molecular Patterns | Interactions | Scoop.it
From molecules to physiology
more...
No comment yet.
Scooped by Gautam Shirsekar
Scoop.it!

The Arabidopsis ZED1 pseudokinase is required for ZAR1-mediated immunity induced by the Pseudomonas syringae type III effector HopZ1a

more...
No comment yet.
Scooped by Gautam Shirsekar
Scoop.it!

Bonding in the Lab | The Scientist Magazine®

Bonding in the Lab | The Scientist Magazine® | Interactions | Scoop.it
How to make your lab less like a factory and more like a family
more...
No comment yet.
Rescooped by Gautam Shirsekar from Plant-microbe interaction
Scoop.it!

Structural Basis for flg22-Induced Activation of the Arabidopsis FLS2-BAK1 Immune Complex

Structural Basis for flg22-Induced Activation of the Arabidopsis FLS2-BAK1 Immune Complex | Interactions | Scoop.it

Flagellin perception in Arabidopsis is through recognition of its highly conserved N-terminal epitope (flg22) by flagellin-sensitive 2 (FLS2). Flg22 binding induces FLS2 heteromerization with BRI1-associated kinase 1 (BAK1) and their reciprocal activation followed by plant immunity. Here, we report the crystal structure of FLS2 and BAK1 ectodomains complexed with flg22 at 3.06 angstroms. A conserved and a nonconserved site from the inner surface of the FLS2 solenoid recognize the C- and N-terminal segment of flg22, respectively, without oligomerization or conformational changes in the FLS2 ectodomain. Besides directly interacting with FLS2, BAK1 acts as a coreceptor by recognizing the C terminus of the FLS2-bound flg22. Our data reveal the molecular mechanisms underlying FLS2-BAK1 complex recognition of flg22 and provide insight into the immune receptor complex activation.


Via Suayib Üstün
more...
No comment yet.
Rescooped by Gautam Shirsekar from Plants and Microbes
Scoop.it!

Trends in Plant Science: Susceptibility to plant disease: more than a failure of host immunity (2013)

Trends in Plant Science: Susceptibility to plant disease: more than a failure of host immunity (2013) | Interactions | Scoop.it

Susceptibility to infectious diseases caused by pathogens affects most plants in their natural habitat and leads to yield losses in agriculture. However, plants are not helpless because their immune system can deal with the vast majority of attackers. Nevertheless, adapted pathogens are able to circumvent or avert host immunity making plants susceptible to these uninvited guests. In addition to the failure of the plant immune system, there are other host processes that contribute to plant disease susceptibility. In this review, we discuss recent studies that show the active role played by the host in supporting disease, focusing mainly on biotrophic stages of infection. Plants attract pathogens, enable their entry and accommodation, and facilitate nutrient provision.


Via Kamoun Lab @ TSL
more...
No comment yet.
Rescooped by Gautam Shirsekar from Plants and Microbes
Scoop.it!

Science: India - Science for All (2013)

Science: India - Science for All (2013) | Interactions | Scoop.it

Can science do more to help the world's poor? India is a test bed for innovative approaches to poverty reduction. India's wheat crop is critical to the nation's food security. Farmers across the country now use their cell phones to send pest sightings and growing conditions to the Directorate of Wheat Research in Karnal, headed by Indu Sharma (pictured).

 

"Scientists have a moral responsibility to help the poor."


Via Kamoun Lab @ TSL
more...
No comment yet.
Rescooped by Gautam Shirsekar from Plant-microbe interaction
Scoop.it!

PLOS Pathogens: Bacterial Effector Activates Jasmonate Signaling by Directly Targeting JAZ Transcriptional Repressors

PLOS Pathogens: Bacterial Effector Activates Jasmonate Signaling by Directly Targeting JAZ Transcriptional Repressors | Interactions | Scoop.it

Gram-negative bacterial pathogens deliver a variety of virulence proteins through the type III secretion system (T3SS) directly into the host cytoplasm. These type III secreted effectors (T3SEs) play an essential role in bacterial infection, mainly by targeting host immunity. However, the molecular basis of their functionalities remains largely enigmatic. Here, we show that the Pseudomonas syringae T3SE HopZ1a, a member of the widely distributed YopJ effector family, directly interacts with jasmonate ZIM-domain (JAZ) proteins through the conserved Jas domain in plant hosts. JAZs are transcription repressors of jasmonate (JA)-responsive genes and major components of the jasmonate receptor complex. Upon interaction, JAZs can be acetylated by HopZ1a through a putative acetyltransferase activity. Importantly,P. syringae producing the wild-type, but not a catalytic mutant of HopZ1a, promotes the degradation of HopZ1-interacting JAZs and activates JA signaling during bacterial infection. Furthermore, HopZ1a could partially rescue the virulence defect of a P. syringae mutant that lacks the production of coronatine, a JA-mimicking phytotoxin produced by a few P. syringaestrains. These results highlight a novel example by which a bacterial effector directly manipulates the core regulators of phytohormone signaling to facilitate infection. The targeting of JAZ repressors by both coronatine toxin and HopZ1 effector suggests that the JA receptor complex is potentially a major hub of host targets for bacterial pathogens.


Via Suayib Üstün
more...
Suayib Üstün's curator insight, November 1, 2013 12:44 AM

And the HopZ1a Story goes on!

Rescooped by Gautam Shirsekar from Plant-microbe interaction
Scoop.it!

Structural Basis for flg22-Induced Activation of the Arabidopsis FLS2-BAK1 Immune Complex

Structural Basis for flg22-Induced Activation of the Arabidopsis FLS2-BAK1 Immune Complex | Interactions | Scoop.it

Flagellin perception in Arabidopsis is through recognition of its highly conserved N-terminal epitope (flg22) by flagellin-sensitive 2 (FLS2). Flg22 binding induces FLS2 heteromerization with BRI1-associated kinase 1 (BAK1) and their reciprocal activation followed by plant immunity. Here, we report the crystal structure of FLS2 and BAK1 ectodomains complexed with flg22 at 3.06 angstroms. A conserved and a nonconserved site from the inner surface of the FLS2 solenoid recognize the C- and N-terminal segment of flg22, respectively, without oligomerization or conformational changes in the FLS2 ectodomain. Besides directly interacting with FLS2, BAK1 acts as a coreceptor by recognizing the C terminus of the FLS2-bound flg22. Our data reveal the molecular mechanisms underlying FLS2-BAK1 complex recognition of flg22 and provide insight into the immune receptor complex activation.


Via Suayib Üstün
more...
No comment yet.
Scooped by Gautam Shirsekar
Scoop.it!

Recent Advances in Calcium/Calmodulin-Mediated Signaling with an Emphasis on Plant-Microbe Interactions http://www.plantphysiol.org/content/163/2/531.full

Recent Advances in Calcium/Calmodulin-Mediated Signaling with an Emphasis on Plant-Microbe Interactions http://www.plantphysiol.org/content/163/2/531.full | Interactions | Scoop.it
more...
No comment yet.
Scooped by Gautam Shirsekar
Scoop.it!

Hormone defense networking in rice: tales from a different world

Hormone defense networking in rice: tales from a different world | Interactions | Scoop.it
more...
No comment yet.
Scooped by Gautam Shirsekar
Scoop.it!

Plant immune response to pathogens differs with changing temperatures

Plant immune response to pathogens differs with changing temperatures | Interactions | Scoop.it
more...
No comment yet.
Scooped by Gautam Shirsekar
Scoop.it!

The Magnaporthe oryzae Effector AvrPiz-t Targets the RING E3 Ubiquitin Ligase APIP6 to Suppress Pathogen-Associated Molecular Pattern–Triggered Immunity in Rice

more...
No comment yet.