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dc.contributor.advisorLoake, Garyen
dc.contributor.advisorSpoel, Stevenen
dc.contributor.authorLi, Yuanen
dc.date.accessioned2017-02-08T16:02:28Z
dc.date.available2017-02-08T16:02:28Z
dc.date.issued2016-06-28
dc.identifier.urihttp://hdl.handle.net/1842/19578
dc.description.abstractSalicylic acid (SA) is essential to the establishment of both local and systemic acquired resistance (SAR) against a wide range of phytopathogens. Isochorismate synthase 1 (ICS1) is the key enzyme involved in the synthesis of SA and it is transcriptionally activated by the regulatory proteins SAR deficient 1 (SARD1) and Calmodulin binding protein 60g (CBP60g). It has been demonstrated previously that the loss-of-function mutant, S-nitrosogluthione reductase 1-3 (gsnor1-3), increased cellular levels of S-nitrosylation. Significantly, accumulation of both free SA and its storage form SA-glucoside (SAG), were substantially reduced, disabling multiple SA-dependent immune responses. However, the molecular mechanism underlying this observation remains to be established. Our data suggests that the transcription of ICS1 and it regulators, SARD and CBP60g, are reduced in the gsnor1-3 mutant, implying that increased cellular S-nitrosylation blunts the expression of ICS1 by reducing the transcription of its activators. We demonstrated that SARD1 is S-nitrosylated in vitro resulting in inhibition of its DNA binding activity. Further, Cys438 of SARD1 was found to be the site of S-nitrosylation, demonstrated by the observation that the SARD1 C438S mutant was insensitive to NO regulation in regard to DNA binding activity.en
dc.language.isoen
dc.publisherThe University of Edinburghen
dc.subjectsalicylic aciden
dc.subjectSARD1en
dc.subjectIsochorismate synthase 1en
dc.subjectCS1en
dc.subjectDNA binding activityen
dc.titleRedox regulation of salicylic acid synthesis in plant immunityen
dc.typeThesis or Dissertationen
dc.type.qualificationlevelDoctoralen
dc.type.qualificationnamePhD Doctor of Philosophyen


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