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Tatiana S. Mucyn

Researcher at University of North Carolina at Chapel Hill

Publications -  12
Citations -  1067

Tatiana S. Mucyn is an academic researcher from University of North Carolina at Chapel Hill. The author has contributed to research in topics: Effector & Operon. The author has an hindex of 12, co-authored 12 publications receiving 894 citations. Previous affiliations of Tatiana S. Mucyn include Sainsbury Laboratory & Norwich Research Park.

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The Tomato NBARC-LRR Protein Prf Interacts with Pto Kinase in Vivo to Regulate Specific Plant Immunity

TL;DR: It is shown that Pto and Prf are coincident in the signal transduction pathway that controls ligand-independent signaling and that the bacterial effectors have evolved to target this coregulatory molecular switch.
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Design of synthetic bacterial communities for predictable plant phenotypes.

TL;DR: It is demonstrated that plant–bacterium binary-association assays inform the design of small synthetic communities with predictable phenotypes in the host and that it is possible to infer causal relationships between microbiota membership and host phenotypes and to use these inferences to rationally design novel communities.
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Genome-wide identification of bacterial plant colonization genes.

TL;DR: Analysis of bacterial genes by sequence-driven saturation mutagenesis revealed a genome-wide map of the genetic determinants of plant root colonization and offers a starting point for targeted improvement of the colonization capabilities of plant-beneficial microbes.
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Prf immune complexes of tomato are oligomeric and contain multiple Pto‐like kinases that diversify effector recognition

TL;DR: Tomato lines containing Prf complexed with Pth proteins but not Pto possessed greater immunity against P. syringae than tomatoes lacking Prf, demonstrating that incorporation of non-Pto kinases into the Prfcomplex extends the number of effector proteins that can be recognized.
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Host inhibition of a bacterial virulence effector triggers immunity to infection.

TL;DR: Here it is shown that Pto is resistant to AvrPtoB-mediated degradation because it inactivates the E3 ligase domain, which is one mechanism by which plants resist disease.