Purification of a Crenarchaeal ATP Synthase in the Light of the Unique Bioenergetics of Ignicoccus Species

Author:

Kreuter Lydia J.1,Weinfurtner Andrea1,Ziegler Alexander1,Weigl Julia1,Hoffmann Jan2,Morgner Nina2,Müller Volker3,Huber Harald1

Affiliation:

1. Institute for Microbiology and Archaeal Center, Regensburg University, Regensburg, Germany

2. Institute of Physical and Theoretical Chemistry, Johann Wolfgang Goethe University, Frankfurt am Main, Germany

3. Department of Molecular Microbiology and Bioenergetics, Johann Wolfgang Goethe University, Frankfurt am Main, Germany

Abstract

The Crenarchaeota represent one of the major phyla within the Archaea domain. This study describes the successful purification of a crenarchaeal ATP synthase. To date, all information about A-type ATP synthases is from euryarchaeal enzymes. The fact that it has not been possible to purify this enzyme complex from a member of the Crenarchaeota until now points to significant differences in stability, possibly caused by structural alterations. Furthermore, the study subject I. hospitalis has a particular importance among crenarchaeotes, since it is the only known host of N. equitans . The energy metabolism in this system is still poorly understood, and our results can help elucidate the unique relationship between these two microbes.

Funder

Deutsche Forschungsgemeinschaft

EC | FP7 | FP7 Ideas: European Research Council

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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