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The Archaeal Sac10b Protein Family: Conserved Proteins with Divergent Functions

Current Protein & Peptide Science, 2012
Here we review the present state of structural and functional studies of the Sac10b protein family, a class of highly conserved 10 kDa nucleic acid-binding proteins in archaea. Based on biochemical and structural studies, these proteins were originally assigned a role in the structural organization of chromatin; Sac10b proteins of hyperthermophilic ...
Jinsong, Xuan, Yingang, Feng
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Investigation of the regulatory function of archaeal ribosomal protein L4

Biochemistry (Moscow), 2014
Ribosomal protein L4 is a regulator of protein synthesis in the Escherichia coli S10 operon, which contains genes of 11 ribosomal proteins. In this work, we have investigated regulatory functions of ribosomal protein L4 of the thermophilic archaea Methanococcus jannaschii. The S10-like operon from M.
A O, Mikhaylina   +6 more
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Structural Dynamics of Archaeal Small Heat Shock Proteins

Journal of Molecular Biology, 2008
Small heat shock proteins (sHsps) are a widespread and diverse class of molecular chaperones. In vivo, sHsps contribute to thermotolerance. Recent evidence suggests that their function in the cellular chaperone network is to maintain protein homeostasis by complexing a variety of non-native proteins.
Martin, Haslbeck   +4 more
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An archaeal chaperonin-based reactor for renaturation of denatured proteins

Extremophiles, 2000
We describe an original chaperonin-based reactor that yields folded and active proteins from denatured materials. We used the 920-kDa chaperonin of the archaeon Sulfolobus solfataricus, which does not require any protein partner for its full activity and assists in vitro folding with low substrate specificity. The reactor consists of an ultrafiltration
L. CERCHIA   +2 more
openaire   +5 more sources

Overexpression of an archaeal protein in yeast: Secretion bottleneck at the ER

Biotechnology and Bioengineering, 2002
AbstractArchaeal enzymes have great potential for industrial use; however, expressing them in their natural hosts has proven challenging. Growth conditions for many archaea are beyond typical fermentation capabilities, and to compound the problem, archaea generally achieve much lower biomass yields than Escherichia coli or Saccharomyces cerevisiae.
Jason D, Smith, Anne Skaja, Robinson
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Structural characterization of the functional regions in the archaeal protein Sso7d

Proteins: Structure, Function, and Bioinformatics, 2007
AbstractSso7d from the extreme thermophilic crenarchaeon Sulfolobus solfataricus is a multifunctional protein in in vitro assays, whose in vivo role is still puzzling. Crystals of Sso7d in complex with DNA elucidated the protein surface involved in the binding to the nucleic acid, whereas the locations of the Sso7d regions responsible for a chaperone ...
Renzone G   +5 more
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Facing extremes: archaeal surface-layer (glyco)proteins

Microbiology, 2003
Archaea are best known in their capacities as extremophiles, i.e. micro-organisms able to thrive in some of the most drastic environments on Earth. The protein-based surface layer that envelopes many archaeal strains must thus correctly assemble and maintain its structural integrity in the face of the physical challenges associated with, for instance ...
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The interplay between nucleoid organization and transcription in archaeal genomes

Nature Reviews Microbiology, 2015
Eveline Peeters   +2 more
exaly  

The archaeal cell envelope

Nature Reviews Microbiology, 2011
Benjamin H Meyer, Sonja-Verena Albers
exaly  

Soluble expression of archaeal proteins in Escherichia coli by using fusion-partners

Protein Expression and Purification, 2008
Seonghun Kim, Sun Bok Lee
exaly  

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