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Insight into the proteome of the hyperthermophilic Crenarchaeon Ignicoccus hospitalis: the major cytosolic and membrane proteins.

Authors :
Burghardt, Tillmann
Saller, Manfred
Gürster, Sonja
Müller, Daniel
Meyer, Carolin
Jahn, Ulrike
Hochmuth, Eduard
Deutzmann, Rainer
Siedler, Frank
Babinger, Patrick
Wirth, Reinhard
Huber, Harald
Rachel, Reinhard
Source :
Archives of Microbiology. Sep2008, Vol. 190 Issue 3, p379-394. 16p. 2 Black and White Photographs, 2 Diagrams, 3 Charts.
Publication Year :
2008

Abstract

Ignicoccus hospitalis, a hyperthermophilic, chemolithoautotrophic Crenarchaeon, is the host of Nanoarchaeum equitans. Together, they form an intimate association, the first among Archaea. Membranes are of fundamental importance for the interaction of I. hospitalis and N. equitans, as they harbour the proteins necessary for the transport of macromolecules like lipids, amino acids, and cofactors between these organisms. Here, we investigated the protein inventory of I. hospitalis cells, and were able to identify 20 proteins in total. Experimental evidence and predictions let us conclude that 11 are soluble cytosolic proteins, eight membrane or membrane-associated proteins, and a single one extracellular. The quantitatively dominating proteins in the cytoplasm (peroxiredoxin; thermosome) antagonize oxidative and temperature stress which I. hospitalis cells are exposed to at optimal growth conditions. Three abundant membrane protein complexes are found: the major protein of the outer membrane, which might protect the cell against the hostile environment, forms oligomeric complexes with pores of unknown selectivity; two other complexes of the cytoplasmic membrane, the hydrogenase and the ATP synthase, play a key role in energy production and conversion. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
03028933
Volume :
190
Issue :
3
Database :
Academic Search Index
Journal :
Archives of Microbiology
Publication Type :
Academic Journal
Accession number :
33770270
Full Text :
https://doi.org/10.1007/s00203-008-0399-x