A5023221161- Glycosylation and Glycoproteins Research
- Genomics and Phylogenetic Studies
- RNA and protein synthesis mechanisms
- Bacterial Genetics and Biotechnology
- Carbohydrate Chemistry and Synthesis
- Bacteriophages and microbial interactions
- Enzyme Structure and Function
- Enzyme Production and Characterization
- Cholinesterase and Neurodegenerative Diseases
- Peptidase Inhibition and Analysis
- Computational Drug Discovery Methods
- RNA modifications and cancer
- Photosynthetic Processes and Mechanisms
- Photoreceptor and optogenetics research
- Microbial Community Ecology and Physiology
- Protist diversity and phylogeny
- Lipid Membrane Structure and Behavior
- Protein Structure and Dynamics
- Microbial Metabolic Engineering and Bioproduction
- Pesticide Exposure and Toxicity
- Spectroscopy Techniques in Biomedical and Chemical Research
- Mitochondrial Function and Pathology
- Microbial Metabolites in Food Biotechnology
- Galectins and Cancer Biology
- Escherichia coli research studies
Ben-Gurion University of the Negev
2016-2025
Duke University Hospital
2017
Duke Medical Center
2017
University of Georgia
2005
Tufts University
2004
Dartmouth College
1995-1998
Hebrew University of Jerusalem
1990-1998
Weizmann Institute of Science
1990-1995
École Normale Supérieure - PSL
1994
École Polytechnique Fédérale de Lausanne
1979
Treatment of bacteria with silver yields intense and highly specific surface-enhanced Raman spectroscopy (SERS) spectra from various cellular chemical components located in the vicinity colloids. In particular, we demonstrate an extreme sensitivity to flavin associated cell envelope their state oxidation. Different spectra, possibly DNA, carboxylates, perhaps phosphates, are obtained soluble interior fraction cell.
Some ionic liquids (ILs) have been shown to be very effective solvents for biomass pretreatment. It is known that some ILs can a strong inhibitory effect on fungal cellulases, making the digestion of cellulose inefficient in presence ILs. The identification IL-tolerant enzymes could produced as cellulase cocktail would reduce costs and water use requirements IL pretreatment process. Due their adaptation high salinity environments, halophilic are hypothesized good candidates screening...
Summary To cope with life in hypersaline environments, halophilic archaeal proteins are enriched acidic amino acids. This strategy does not, however, offer a response to transient changes salinity, as would post‐translational modifications. test this hypothesis, N‐glycosylation of the Haloferax volcanii S‐layer glycoprotein was compared cells grown high (3.4 M NaCl) and low (1.75 salt, glycan bound dolichol phosphate, lipid upon which N‐linked is assembled. In Asn‐13 Asn‐83 modified by...
Abstract The swimming device of archaea—the archaellum—presents asparagine (N)-linked glycans. While N-glycosylation serves numerous roles in archaea, including enabling their survival extreme environments, how this post-translational modification contributes to cell motility remains under-explored. Here, we report the cryo-EM structure archaellum filaments from haloarchaeon Halobacterium salinarum , where archaellins, building blocks archaellum, are N-glycosylated, and pathway is...
The transport of large preproteins across the Escherichia coli plasma membrane is catalyzed by preprotein translocase, comprised peripherally bound SecA subunit and an integrally heterotrimeric domain consisting SecY, SecE, SecG subunits. We have now placed secY, secE, secG genes under control arabinose-inducible promoter on a multicopy plasmid. Upon induction, all three proteins are strongly overexpressed recovered in fraction. These membranes show strong enhancement 1) translocation ATPase...
In this study, characterization of the N-glycosylation process in haloarchaea Haloferax volcanii was undertaken. Initially, putative Hfx. homologues genes involved eukaryal or bacterial were identified by bioinformatics. Reverse transcription polymerase chain reaction (RT-PCR) confirmed that proposed are transcribed, indicative true proteins being encoded. Where families related gene sequences detected, differential family members under a variety physiological and environmental conditions...
In Archaea, dolichol phosphates have been implicated as glycan carriers in the N-glycosylation pathway, much like their eukaryal counterparts. To clarify this relation, highly sensitive liquid chromatography/mass spectrometry was employed to detect and characterize glycan-charged phosphodolichols haloarchaeon Haloferax volcanii. It is reported that Hfx. volcanii contains a series of C(55) C(60) presenting saturated isoprene subunits at α ω positions sequentially modified with first, second,...
The ability of Eukarya, Bacteria and Archaea to perform N-glycosylation underlies the importance possible antiquity this post-translational protein modification. However, in contrast relatively well-studied eukaryal bacterial pathways, archaeal process is less understood. To remedy disparity, following study has examined 56 available genomes with aim identifying glycosyltransferases oligosaccharyltransferases, including those putatively catalyzing processing event. This analysis reveals that...
N-glycosylation in Archaea presents aspects of this posttranslational modification not seen either Eukarya or Bacteria. In the haloarchaeon Haloferax volcanii, surface (S)-layer glycoprotein can be simultaneously modified by two different N-glycans. Asn-13 and Asn-83 are a pentasaccharide, whereas Asn-498 is tetrasaccharide distinct composition, with at position being related to environmental conditions. Specifically, detected when cells grown presence 1.75 but 3.4 M NaCl. While deletion...
ABSTRACT Despite providing the first example of archaeal N-glycosylation almost 50 years ago, detailed insight into pathway used by Halobacterium salinarum to assemble and attach an N-linked tetrasaccharide decorating glycoproteins in this haloarchaea has only recently appeared. Still, numerous components remain be identified, including sulfotransferase(s), which modify third fourth sugars. In present report, a series bioinformatics, genetic, biochemical, structural approaches served reveal...
Archaea, like Eukarya and Bacteria, are able to N glycosylate select protein targets. However, in contrast relatively advanced understanding of the eukaryal glycosylation process information being amassed on bacterial process, little is known this posttranslational modification Archaea. Toward remedying situation, present report continues ongoing efforts identify components involved Haloferax volcanii S-layer glycoprotein. By combining gene deletion together with mass spectrometry, AglE,...
Proteins in all three domains of life can experience N-glycosylation. The steps involved the archaeal version this post-translational modification remain largely unknown. Hence, as next step ongoing efforts to identify components N-glycosylation pathway halophilic archaeon Haloferax volcanii, involvement additional gene products biosynthesis pentasaccharide decorating S-layer glycoprotein was demonstrated. genes encoding AglF, AglI and AglG are found immediately upstream oligosaccharide...
Like the Eukarya and Bacteria, Archaea also perform N glycosylation. Using haloarchaeon Haloferax volcanii as a model system, series of Agl proteins involved in archaeal version this posttranslational modification has been identified. In present study, participation HVO_1517 glycosylation was considered, given its homology to known component eukaryal N-glycosylation pathway because genomic proximity agl genes encoding elements H. process. By combining deletion with mass spectrometric...
Like Eukarya and Bacteria, Archaea are also capable of performing N-glycosylation. In the halophilic archaeon Haloferax volcanii, N-glycosylation is mediated by products agl gene cluster. present report, this cluster was expanded to include an additional sequence, aglM, shown participate in biosynthesis hexuronic acids contained within a pentasaccharide decorating S-layer glycoprotein, reporter H. volcanii glycoprotein. response different growth conditions, changes transcription profile aglM...