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Rutledge final seminar presentation.pptx Public Deposited

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  • To initiate the defense response to an invading pathogen, plants utilize an array of immune receptors to recognize virulence effectors. Virulence effectors are released by pathogens to suppress immune responses in target hosts. These effectors are recognized by a family of resistance proteins known as nucleotide-binding leucine-rich repeat (NB-LRR) proteins. Past research has shown these NB-LRR proteins localize to and exert their function in the cell nucleus through transcriptional re-programming. The Arabidopsis thaliana LOV1 gene produces a NB-LRR protein that confers sensitivity to the host-selective toxin, victorin, produced by Cochliobolus victoriae. When LOV1 is expressed in Arabidopsis or Nicotiana benthamiana, exposure to victorin elicits the hypersensitive response (HR), which is typically associated with the plant defense response. In this study, we show that LOV1 localizes to and exerts its function in the plasma membrane, and does not require nuclear localization in Nicotiana benthamiana. Preventing nuclear entry of LOV1 did not affect its ability to mediate the victorin-induced HR, supporting the hypothesis that LOV1 does not require nuclear localization. Inhibiting de novo transcription of defense genes by use of an adenosine analog, cordycepin, showed no difference in the ability of LOV1 to confer HR cell death, indicating that the LOV1 response does not involve transcriptional reprogramming. Tethering LOV1 irreversibly to the plasma membrane with a dual acylated N-terminal tag did not impact its ability to mediate HR cell death, reinforcing the idea that LOV1 signaling occurs at the plasma membrane. This research supports the idea that plant NB-LRR proteins can exert their effector-mediated HR function without nuclear localization.
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  • description.provenance : Made available in DSpace on 2013-07-19T21:55:39Z (GMT). No. of bitstreams: 2Rutledge final seminar presentation.pptx: 12777842 bytes, checksum: 5c1c1109d3b959cadbeb098c03919171 (MD5)Rutledge Patrick - Research Thesis Final (June 11 2013) .pdf: 632804 bytes, checksum: 03581744ddab2db6d9e508b3b15bd135 (MD5)
  • description.provenance : Submitted by Wanda Crannell (brr@oregonstate.edu) on 2013-07-17T21:07:58ZNo. of bitstreams: 2Rutledge final seminar presentation.pptx: 12777842 bytes, checksum: 5c1c1109d3b959cadbeb098c03919171 (MD5)Rutledge Patrick - Research Thesis Final (June 11 2013) .pdf: 632804 bytes, checksum: 03581744ddab2db6d9e508b3b15bd135 (MD5)
  • description.provenance : Approved for entry into archive by Deanne Bruner(deanne.bruner@oregonstate.edu) on 2013-07-19T21:55:39Z (GMT) No. of bitstreams: 2Rutledge final seminar presentation.pptx: 12777842 bytes, checksum: 5c1c1109d3b959cadbeb098c03919171 (MD5)Rutledge Patrick - Research Thesis Final (June 11 2013) .pdf: 632804 bytes, checksum: 03581744ddab2db6d9e508b3b15bd135 (MD5)

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