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Deep Sea Microbes Probed by Incoherent Neutron Scattering Under High Hydrostatic Pressure ArchiMer
Peters, Judith; Martinez, Nicolas; Michoud, Gregoire; Carlo, Anais; Franzetti, Bruno; Oger, Philippe; Jebbar, Mohamed.
The majority of the biosphere is a high pressure environment. Around 70% of the marine biosphere lies at depths below 1000 m, i.e. at pressures of 100 bars or higher. To survive in these environments, deep-biosphere organisms have adapted to life at high pressure. In vitro studies showed that the activity of certain proteins originating from deep-sea organisms is less affected by high pressure than that of enzymes from surface organisms [1-3]. However, the genetic and structural bases for this increased pressure resistance are still unknown. Elastic incoherent neutron scattering studies, which provide access to information about molecular dynamics, constitute a very promising approach to decipher the structural adaptation in proteins living under high...
Tipo: Text Palavras-chave: Neutron Scattering; Molecular Dynamics; High Pressure; Deep Sea Microbes.
Ano: 2014 URL: http://archimer.ifremer.fr/doc/00251/36186/34725.pdf
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Pyrococcus horikoshii TET2 Peptidase Assembling Process and Associated Functional Regulation ArchiMer
Appolaire, Alexandre; Rosenbaum, Eva; Dura, M. Asuncion; Colombo, Matteo; Marty, Vincent; Savoye, Marjolaine Noirclerc; Godfroy, Anne; Schoehn, Guy; Girard, Eric; Gabel, Frank; Franzetti, Bruno.
Tetrahedral (TET) aminopeptidases are large polypeptide destruction machines present in prokaryotes and eukaryotes. Here, the rules governing their assembly into hollow 12-subunit tetrahedrons are addressed by using TET2 from Pyrococcus horikoshii (PhTET2) as a model. Point mutations allowed the capture of a stable, catalytically active precursor. Small angle x- ray scattering revealed that it is a dimer whose architecture in solution is identical to that determined by x- ray crystallography within the fully assembled TET particle. Small angle x- ray scattering also showed that the reconstituted PhTET2 dodecameric particle displayed the same quaternary structure and thermal stability as the wild-type complex. The PhTET2 assembly intermediates were...
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Ano: 2013 URL: http://archimer.ifremer.fr/doc/00177/28820/27491.pdf
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