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

Burghardt, Tillmann and Saller, Manfred and Gürster, Sonja and Müller, Daniel and Meyer, Carolin and Jahn, Ulrike and Hochmuth, Eduard and Deutzmann, Rainer and Siedler, Frank and Babinger, Patrick and Wirth, Reinhard and Huber, Harald and Rachel, Reinhard (2008) Insight into the proteome of the hyperthermophilic Crenarchaeon Ignicoccus hospitalis: the major cytosolic and membrane proteins. Archives of microbiology 190 (3), pp. 379-394.

Full text not available from this repository.

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.

Item Type:Article
Institutions: Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie > Prof. Dr. Michael Thomm
Identification Number:
ValueType
9226896PubMed ID
10.1007/s00203-008-0399-xDOI
Classification:
NotationType
Archaeal Proteins/chemistryMESH
Computational BiologyMESH
Cytosol/chemistryMESH
Desulfurococcaceae/chemistryMESH
Electrophoresis, Polyacrylamide GelMESH
Membrane Proteins/chemistryMESH
Proteome/chemistryMESH
Spectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationMESH
Tandem Mass SpectrometryMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Owner:Gertraud Kellers
Deposited On:05 Mar 2010 09:29
Last Modified:05 Mar 2010 09:29
Item ID:13220
Export bibliographical data
Literature of the same author
plusin this repository
plusat BASE
plusat Google Scholar
plusat Scirus
plusat PubMed

at PubMed

at publisher (via DOI)

Bookmark
Owner Only: item control page