Analysis of succinate dehydrogenase subunit 1 in mitochondrial plant stress signaling and investigation of SDHAF4 as a new assembly factor for SDH1

Katharina Belt

Research output: ThesisDoctoral Thesis

Abstract

Plants are sessile organisms and as such are exposed to many kinds of environments and pathogens that cause stress. Therefore, an efficient plant stress response to these abiotic or biotic threats is important. Within this thesis, the mitochondrial enzyme succinate dehydrogenase (SDH) and in particular the SDH1 subunit was found to be involved in plant stress signaling. Stress response to the chemical signal salicylic acid was decreased in SDH1 mutant plants. To ensure functional stress response, SDH1 needs to be assembled correctly into the SDH halo-complex. A new protein in SDH1 assembly machinery in plants was discovered.
LanguageEnglish
QualificationDoctor of Philosophy
Awarding Institution
  • The University of Western Australia
Supervisors/Advisors
  • Millar, Andrew, Supervisor
  • Huang, Shaobai, Supervisor
  • Van Aken, Olivier, Supervisor
  • Small, Ian, Supervisor
Thesis sponsors
Award date24 Jan 2018
DOIs
Publication statusUnpublished - 2018

Fingerprint

plant stress
stress response
succinate dehydrogenase (quinone)
salicylic acid
mutants
pathogens
organisms
enzymes
fumarate reductase (quinol)
proteins

Cite this

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title = "Analysis of succinate dehydrogenase subunit 1 in mitochondrial plant stress signaling and investigation of SDHAF4 as a new assembly factor for SDH1",
abstract = "Plants are sessile organisms and as such are exposed to many kinds of environments and pathogens that cause stress. Therefore, an efficient plant stress response to these abiotic or biotic threats is important. Within this thesis, the mitochondrial enzyme succinate dehydrogenase (SDH) and in particular the SDH1 subunit was found to be involved in plant stress signaling. Stress response to the chemical signal salicylic acid was decreased in SDH1 mutant plants. To ensure functional stress response, SDH1 needs to be assembled correctly into the SDH halo-complex. A new protein in SDH1 assembly machinery in plants was discovered.",
keywords = "Mitochondria, Assembly , Stress signalling, SDH1, Succinate dehydrogenase, Arabidopsis , Salicylic acid, SDHAF1",
author = "Katharina Belt",
year = "2018",
doi = "10.4225/23/5a7bed8135d86",
language = "English",
school = "The University of Western Australia",

}

TY - THES

T1 - Analysis of succinate dehydrogenase subunit 1 in mitochondrial plant stress signaling and investigation of SDHAF4 as a new assembly factor for SDH1

AU - Belt, Katharina

PY - 2018

Y1 - 2018

N2 - Plants are sessile organisms and as such are exposed to many kinds of environments and pathogens that cause stress. Therefore, an efficient plant stress response to these abiotic or biotic threats is important. Within this thesis, the mitochondrial enzyme succinate dehydrogenase (SDH) and in particular the SDH1 subunit was found to be involved in plant stress signaling. Stress response to the chemical signal salicylic acid was decreased in SDH1 mutant plants. To ensure functional stress response, SDH1 needs to be assembled correctly into the SDH halo-complex. A new protein in SDH1 assembly machinery in plants was discovered.

AB - Plants are sessile organisms and as such are exposed to many kinds of environments and pathogens that cause stress. Therefore, an efficient plant stress response to these abiotic or biotic threats is important. Within this thesis, the mitochondrial enzyme succinate dehydrogenase (SDH) and in particular the SDH1 subunit was found to be involved in plant stress signaling. Stress response to the chemical signal salicylic acid was decreased in SDH1 mutant plants. To ensure functional stress response, SDH1 needs to be assembled correctly into the SDH halo-complex. A new protein in SDH1 assembly machinery in plants was discovered.

KW - Mitochondria

KW - Assembly

KW - Stress signalling

KW - SDH1

KW - Succinate dehydrogenase

KW - Arabidopsis

KW - Salicylic acid

KW - SDHAF1

U2 - 10.4225/23/5a7bed8135d86

DO - 10.4225/23/5a7bed8135d86

M3 - Doctoral Thesis

ER -