KOPS - Das Institutionelle Repositorium der Universität Konstanz

Amylase MalS und Protease DegP aus Escherichia coli: Faltung und Abbau unter Kontrolle der Temperatur

Amylase MalS und Protease DegP aus Escherichia coli: Faltung und Abbau unter Kontrolle der Temperatur

Zitieren

Dateien zu dieser Ressource

Prüfsumme: MD5:be998de06ddc816a6da4a3b965bea5e8

SPIESS, Christoph, 1999. Amylase MalS und Protease DegP aus Escherichia coli: Faltung und Abbau unter Kontrolle der Temperatur [Dissertation]. Konstanz: University of Konstanz

@phdthesis{Spiess1999Amyla-7818, title={Amylase MalS und Protease DegP aus Escherichia coli: Faltung und Abbau unter Kontrolle der Temperatur}, year={1999}, author={Spiess, Christoph}, address={Konstanz}, school={Universität Konstanz} }

1999 Amylase MalS und Protease DegP aus Escherichia coli: Faltung und Abbau unter Kontrolle der Temperatur deposit-license 2011-03-24T17:37:46Z application/pdf Spiess, Christoph In contrast to protein folding in the cytoplasm of Escherichia coli the folding of proteins in the periplasm is insufficiently examined and not well understood. Only some folding catalysts and a few specialized chaperones are identified so far. Nothing is known about the existence of a general molecular chaperone.<br />In this work periplasmic amylase MalS was used as a model system to study the folding path and conditions of periplasmic proteins. Formation of two disulfide bonds is a prerequisite for proper folding of MalS. Disulfidebond formation is catalyzed in the periplasm by the disulfideoxidase DsbA. In absence of DsbA folding of MalS is inefficent at temperatures above 30 °C. Reduced MalS is degraded efficiently by the periplasmic protease DegP. At temperatures below 30 °C folding in absence of DsbA is much more efficient but dependent on the protease DegP. These in vivo results were completed by in vitro experiments using the purified compounds. The results revealed that protease DegP has chaperone activity at low temperatures. At elevated temperatures the protease activity is overriding the chaperone. Thus protease DegP is a bifunctional protein. As a central player it has to decide between two contrary solutions for proteins in trouble: folding or degradation! 2011-03-24T17:37:46Z Spiess, Christoph deu Amylase MalS and protease DegP of Escherichia coli: folding and degradation under control of the temperature

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

398_1.pdf 255

Das Dokument erscheint in:

KOPS Suche


Stöbern

Mein Benutzerkonto