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

@article{citeulike:2940889, 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.}, address = {Centre for Electron Microscopy, Faculty for Biology and Preclinical Medicine, University of Regensburg, Universit\"{a}tsstra{\ss}e 31, 93053, Regensburg, Germany.}, author = {Burghardt, Tillmann and Saller, Manfred and G\"{u}rster, Sonja and M\"{u}ller, 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 }, citeulike-article-id = {2940889}, doi = {http://dx.doi.org/10.1007/s00203-008-0399-x}, issn = {0302-8933}, journal = {Archives of microbiology}, keywords = {archaea, cytosol, ignicoccus, membrane, proteomics}, month = {June}, posted-at = {2008-06-29 04:48:48}, priority = {2}, title = {Insight into the proteome of the hyperthermophilic Crenarchaeon Ignicoccus hospitalis: the major cytosolic and membrane proteins.}, url = {http://dx.doi.org/10.1007/s00203-008-0399-x}, year = {2008} }

TY - JOUR ID - citeulike:2940889 L3 - citeulike-article-id:2940889 TI - Insight into the proteome of the hyperthermophilic Crenarchaeon Ignicoccus hospitalis: the major cytosolic and membrane proteins. JF - Archives of microbiology AD - Centre for Electron Microscopy, Faculty for Biology and Preclinical Medicine, University of Regensburg, Universitätsstraße 31, 93053, Regensburg, Germany. SN - 0302-8933 N2 - 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. KW - archaea KW - cytosol KW - ignicoccus KW - membrane KW - proteomics AU - Burghardt, Tillmann AU - Saller, Manfred AU - Gürster, Sonja AU - Müller, Daniel AU - Meyer, Carolin AU - Jahn, Ulrike AU - Hochmuth, Eduard AU - Deutzmann, Rainer AU - Siedler, Frank AU - Babinger, Patrick AU - Wirth, Reinhard AU - Huber, Harald AU - Rachel, Reinhard PY - 2008/06/27/ UR - http://dx.doi.org/10.1007/s00203-008-0399-x ER -