Experimental limit on an exotic parity-odd spin- and velocity-dependent interaction using an optically polarized vapor

Porphyrins are key elements in organic-inorganic hybrid systems for a wide range of applications. Understanding their interaction with the substrate gives a handle on structural and electronic device properties. Here...

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Pathogen effector recognition-dependent association of NRG1 with EDS1 and SAG101 in TNL receptor immunity

Nature Communications ◽

10.1038/s41467-021-23614-x ◽

2021 ◽

Vol 12 (1) ◽

Author(s):

Xinhua Sun ◽

Dmitry Lapin ◽

Joanna M. Feehan ◽

Sara C. Stolze ◽

Katharina Kramer ◽

...

Keyword(s):

Disease Susceptibility ◽

Nucleotide Binding ◽

Molecular Evidence ◽

Pathogen Effectors ◽

Pathogen Effector ◽

Family Protein ◽

Activated State ◽

Defence Signalling ◽

Effector Recognition ◽

Dependent Interaction

AbstractPlants utilise intracellular nucleotide-binding, leucine-rich repeat (NLR) immune receptors to detect pathogen effectors and activate local and systemic defence. NRG1 and ADR1 “helper” NLRs (RNLs) cooperate with enhanced disease susceptibility 1 (EDS1), senescence-associated gene 101 (SAG101) and phytoalexin-deficient 4 (PAD4) lipase-like proteins to mediate signalling from TIR domain NLR receptors (TNLs). The mechanism of RNL/EDS1 family protein cooperation is not understood. Here, we present genetic and molecular evidence for exclusive EDS1/SAG101/NRG1 and EDS1/PAD4/ADR1 co-functions in TNL immunity. Using immunoprecipitation and mass spectrometry, we show effector recognition-dependent interaction of NRG1 with EDS1 and SAG101, but not PAD4. An EDS1-SAG101 complex interacts with NRG1, and EDS1-PAD4 with ADR1, in an immune-activated state. NRG1 requires an intact nucleotide-binding P-loop motif, and EDS1 a functional EP domain and its partner SAG101, for induced association and immunity. Thus, two distinct modules (NRG1/EDS1/SAG101 and ADR1/EDS1/PAD4) mediate TNL receptor defence signalling.

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Mg X ATP2-dependent interaction of the inhibitor protein of the cAMP-dependent protein kinase with the catalytic subunit.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)32719-4 ◽

1983 ◽

Vol 258 (6) ◽

pp. 3682-3692 ◽

Cited By ~ 13

Author(s):

S Whitehouse ◽

D A Walsh

Keyword(s):

Protein Kinase ◽

Catalytic Subunit ◽

Inhibitor Protein ◽

Dependent Protein Kinase ◽

Camp Dependent Protein Kinase ◽

Dependent Protein ◽

Dependent Interaction

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Interactions of Drosophila Ultrabithorax Regulatory Regions With Native and Foreign Promoters

Genetics ◽

10.1093/genetics/145.1.123 ◽

1997 ◽

Vol 145 (1) ◽

pp. 123-137 ◽

Cited By ~ 5

Author(s):

Fernando Casares ◽

Welcome Bender ◽

John Merriam ◽

Ernesto Sánchez-Herrero

Keyword(s):

P Element ◽

Lacz Gene ◽

Bithorax Complex ◽

Lacz Reporter ◽

Normal Pattern ◽

Lacz Reporter Gene ◽

Regulatory Regions ◽

Long Range Interactions ◽

In Trans ◽

Dependent Interaction

The Ultrabithorax (Ubx) gene of the Drosophila bithorax complex is required to specify parasegments 5 and 6. Two P-element “enhancer traps” have been recovered within the locus that contain the bacterial lacZ gene under the control of the P-element promoter. The P insertion that is closer to the Ubx promoter expresses lucZ in a pattern similar to that of the normal Ubx gene, but also in parasegment 4 during embryonic development. Two deletions have been recovered that remove the normal Ubx promoter plus several kilobases on either side, but retain the lacZ reporter gene. The lacZ patterns from the deletion derivatives closely match the normal pattern of Ubx expression in late embryos and imaginal discs. The lacZ genes in the deletion derivatives are also negatively regulated by Ubx and activated in trans by Contrabithorax mutations, again like the normal Ubx gene. Thus, the deleted regions, including several kilobases around the Ubx promoter, are not required for long range interactions with Ubx regulatory regions. The deletion derivatives also stimulate transvection, a pairing-dependent interaction with the Ubx promoter on the homologous chromosome.

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