Biochemical and physiological characterisation of Deg/HtrA proteases in Synechocystis sp. PCC 6803

Perthold, Manuela

Biochemical and physiological characterisation of Deg/HtrA proteases in Synechocystis sp. PCC 6803

Dateien

Perthold_280910.pdf(3.9 MB)

Datum

2014

Publikationstyp

Dissertation

Zusammenfassung

Deg/HtrA proteases are ATP-independent endoproteases that can be found in almost every organism and possess, besides a protease domain with a catalytically active serine residue, up to four PDZ domains, which mediate i.a. copmlex formation. The three Deg/HtrA proteases HhoA, HtrA and HhoB in Synechocystis sp. PCC 6803 are of special interest, because they combine features of their plant and bacterial homologues and are thought to be involved in responses to abiotic stresses and turnover of the PSII reaction centre protein D1. This study focused on the role of the cyanobacterial Deg/HtrA proteases in the short-term response to elevated salt concentrations, particularly on changes in levels of photosynthesis-related proteins and florescence kinetics. Furthermore, state-of-the-art methods for substrate identification were tested for their practicability in cyanobacteria and the role of the PDZ domain in the oligomerisation process was determined.

Zusammenfassung in einer weiteren Sprache

Deg/HtrA-Proteasen sind ATP-unabhängige Endoproteasen, die in fast jedem Organismus vorkommen. Neben der Proteasendomäne mit dem katalytisch aktiven Serin besitzen sie bis zu vier PDZ-Domänen, die unter anderem an der Komplexbildung beteiligt sind.
Die drei Deg/HtrA-Proteasen HhoA, HtrA und HhoB in Synechocystis sp. PCC 6803 sind von besonderem Interesse, da diese Proteasen sowohl pflanzliche als auch bakterielle Merkmale aufweisen und möglicherweise eine Rolle in der Antwort auf abiotischen Stress spielen, sowie am Umsatz des PSII-Reaktionszentrums-Proteins D1 beteiligt sein könnten.
Der Fokus dieser Arbeit lag auf der Beteiligung der cyanobakteriellen Deg/HtrA-Proteasen an der Kurzzeit-Antwort auf erhöhte Salzkonzentrationen, vor allem in Bezug auf Photosynthese-relevante Proteine und Fluoreszenzkinetik. Weiterhin wurden neueste Techniken zur Substratidentifikation auf ihre Anwendbarkeit in Cyanobakterien getestet und die Rolle der PDZ-Domäne im Oligomerisierungsprozess wurde bestimmt.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

Proteasen,PDZ-Domäne,Fluoreszenzkinetik,Oligomerisierung

Zitieren

ISO 690

PERTHOLD, Manuela, 2014. Biochemical and physiological characterisation of Deg/HtrA proteases in Synechocystis sp. PCC 6803 [Dissertation]. Konstanz: University of Konstanz

BibTex

@phdthesis{Perthold2014Bioch-28091,
  year={2014},
  title={Biochemical and physiological characterisation of Deg/HtrA proteases in Synechocystis sp. PCC 6803},
  author={Perthold, Manuela},
  address={Konstanz},
  school={Universität Konstanz}
}

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    <dcterms:abstract xml:lang="eng">Deg/HtrA proteases are ATP-independent endoproteases that can be found in almost every organism and possess, besides a protease domain with a catalytically active serine residue, up to four PDZ domains, which mediate i.a. copmlex formation. The three Deg/HtrA proteases HhoA, HtrA and HhoB in Synechocystis sp. PCC 6803 are of special interest, because they combine features of their plant and bacterial homologues and are thought to be involved in responses to abiotic stresses and turnover of the PSII reaction centre protein D1. This study focused on the role of the cyanobacterial Deg/HtrA proteases in the short-term response to elevated salt concentrations, particularly on changes in levels of photosynthesis-related proteins and florescence kinetics. Furthermore, state-of-the-art methods for substrate identification were tested for their practicability in cyanobacteria and the role of the PDZ domain in the oligomerisation process was determined.</dcterms:abstract>
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Prüfungsdatum der Dissertation

April 25, 2014