• Publications
  • Influence
Protein glycosylation in Archaea: sweet and extreme.
TLDR
Current understanding of N-glycosylation in Archaea is described and insight into the biosynthesis and attachment ofN-linked glycans decorating archaeal glycoproteins is starting to amass.
Posttranslational Protein Modification in Archaea
TLDR
The various posttranslational modifications experienced by archaeal proteins, the molecular steps leading to these modifications, and the role played by postTranslational modification in Archaea form the focus of this review.
SecYEG and SecA Are the Stoichiometric Components of Preprotein Translocase (*)
TLDR
Data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase, and that all three of the proteins are strongly overexpressed and recovered in the plasma membrane fraction.
N-Linked Glycosylation in Archaea: a Structural, Functional, and Genetic Analysis
TLDR
Advances in the study of the archaeal version of this important pathway have been made for halophiles, methanogens, and thermoacidophilia, combining glycan structural information obtained by mass spectrometry with bioinformatic, genetic, biochemical, and enzymatic data.
Surface-Enhanced Raman Spectroscopy as a Tool for Probing Specific Biochemical Components in Bacteria
TLDR
This work demonstrates an extreme sensitivity to flavin components associated with the cell envelope and to their state of oxidation in bacteria with silver.
Biotechnological uses of archaeal extremozymes.
  • J. Eichler
  • Biology, Engineering
    Biotechnology advances
  • 1 July 2001
Extreme sweetness: protein glycosylation in archaea
  • J. Eichler
  • Biology
    Nature Reviews Microbiology
  • 1 March 2013
Although N-glycosylation was first reported in archaea almost 40 years ago, detailed insights into this process have become possible only recently, with the availability of complete genome sequences
Identification of a haloalkaliphilic and thermostable cellulase with improved ionic liquid tolerance
TLDR
Interestingly, the tolerances to heat, alkali and ILs are found to be salt-dependent, suggesting that the enzyme is stabilized by the presence of salt.
Endogenous SecA Catalyzes Preprotein Translocation at SecYEG*
TLDR
It is concluded that SecA functions in preprotein translocation only through cycling at SecYEG, and the translocation supported by either endogenous or added SecA is blocked by azide or by antibody to SecY.
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