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FtsH proteases located in the plant chloroplast
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2012 (English)In: Physiologia Plantarum: An International Journal for Plant Biology, ISSN 0031-9317, E-ISSN 1399-3054, Vol. 145, no 1, 203-214 p.Article in journal (Refereed) Published
Abstract [en]

FtsHs are a well-characterized family of membrane bound proteases containing an AAA (ATPase associated with various cellular activities) and a Zn2+ metalloprotease domain. FtsH proteases are found in eubacteria, animals and plants, and are known to have a crucial role in housekeeping proteolysis of membrane proteins. In Arabidopsis thaliana 12 FtsH family members are present (FtsH 1–12) and their subcellular localization is restricted to mitochondria and chloroplasts. In addition, five genes coding for proteins homologous to FtsH (FtsHi 1–5) have been detected in the genome, lacking the conserved zinc-binding motif HEXXH, which presumably renders them inactive for proteolysis. These inactive FtsHs as well as nine of the active FtsHs are thought to be localized in the chloroplast. In this minireview we shortly summarize the recent findings on plastidic FtsH proteases in text and figures. We will mainly focus on FtsH 1, 2, 5 and 8, localized in the thylakoid membrane and known for their importance in photosynthesis.

Place, publisher, year, edition, pages
Oxford: Wiley-Blackwell, 2012. Vol. 145, no 1, 203-214 p.
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:umu:diva-50197DOI: 10.1111/j.1399-3054.2011.01548.xISI: 000302802900021OAI: oai:DiVA.org:umu-50197DiVA: diva2:460071
Available from: 2011-11-29 Created: 2011-11-29 Last updated: 2017-12-08Bibliographically approved
In thesis
1. Characterization of FtsH proteases in the annual plant Arabidopsis thaliana
Open this publication in new window or tab >>Characterization of FtsH proteases in the annual plant Arabidopsis thaliana
2012 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Background FtsH is an ATP-dependent membrane-bound metalloprotease. A. thaliana contains 12 FtsH proteases localized in membranes of chloroplasts and mitochondria where they form homo- or hetero-hexameric complexes. FtsH11 – the main subject of this thesis – is located in the chloroplast envelope.

 

Methods

  • Field studies with A. thaliana to determine Darwinian fitness. A growth under outdoor conditions often allows discovering of phenotypes that are unascertainable in the controlled environment of growth chambers.
  • Proteomic methods to discover fragments of substrate proteins (limited proteolysis) and changes in the proteome of FtsH protease deficient mutants.

 

Results ftsh11 has increased amount of: RuBisCO activase, several Calvin cycle enzymes, two enzymes involved in starch synthesis and some chaperons. Some of those enzymes have been identified as possible substrates of FtsH11. Under long photoperiods ftsh11 develops a chlorotic phenotype accompanied by decreasing NADP+/NADPH ratio and increase of ROS damaged proteins. 

Place, publisher, year, edition, pages
Umeå: Umeå universitet, 2012. 38 p.
National Category
Biological Sciences Chemical Sciences
Research subject
Biochemistry
Identifiers
urn:nbn:se:umu:diva-55161 (URN)978-91-7459-445-4 (ISBN)
Public defence
2012-06-01, KBC-huset, KB3A9, Umeå universitet, Umeå, 10:00 (English)
Opponent
Supervisors
Available from: 2012-05-11 Created: 2012-05-09 Last updated: 2012-05-10Bibliographically approved

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Wagner, RaikAigner, HaraldFunk, Christiane
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