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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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Overexpression of archaeal proteins in Escherichia coli

Biotechnology Letters, 1998
Six archaeal proteins containing a high number of Escherichia coli rare codons in their genes were not well expressed in E. coli. These genes showed a five to twenty-fold increase in production when expressed in the presence of a plasmid harboring and expressing the argU and ileX genes encoding rare tRNAs (tRNA arg(de)AGA/AGG and tRNA ile(de)AUA ...
Rosalind Kim   +5 more
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Archaeal DNA Binding Proteins and Chromosome Structure

Systematic and Applied Microbiology, 1993
Summary Small, basic, abundant DNA-binding proteins have been isolated from many different prokaryotes. Proteins of this type that have been characterized from Archaea are reviewed here, and their structural and functional relationships to bacterial histone-like proteins and eukaryal histones are discussed. Members of the HMf family of archaeal DNA-
Rowan A. Grayling   +2 more
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Sec61β – a component of the archaeal protein secretory system

Trends in Biochemical Sciences, 2002
Sec61p/SecYEG complexes mediate protein translocation across membranes and are present in both eukaryotes and bacteria. Whereas homologues of Sec61alpha/SecY and Sec61gamma/SecE exist in archaea, identification of the third component (Sec61beta or SecG) has remained elusive. Using PSI-BLAST, the archaeal counterpart of Sec61beta has been detected. With
Lisa N, Kinch   +2 more
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Archaeal chromatin proteins: different structures but common function?

Current Opinion in Microbiology, 2005
Chromatin proteins promote chromosome flexibility in vivo, maintaining a compact yet decondensed template that permits polymerase accessibility. All Archaea have at least two types of chromatin proteins, and diversity in the chromatin protein population appears to prevent polymerization of a single type of protein.
Kathleen, Sandman, John N, Reeve
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