Whereas N-glycosylation is a posttranslational modification performed across evolution, the archaeal version of this protein-processing event presents a degree of diversity not seen in either bacteria or eukarya. Accordingly, archaeal N-glycosylation relies on a large number of enzymes that are often species-specific or restricted to a select group of species. As such, there is a need for an organized platform upon which amassing information about archaeal glycosylation (agl) genes can rest. Accordingly, the aglgenes database provides detailed descriptions of experimentally characterized archaeal N-glycosyation pathway components. For each agl gene, genomic information, supporting literature and relevant external links are provided at a functional intuitive web-interface designed for data browsing. Routine updates ensure that novel experimental information on genes and proteins contributing to archaeal N-glycosylation is incorporated into aglgenes in a timely manner. As such, aglgenes represents a specialized resource for sharing validated experimental information online, providing support for workers in the field of archaeal protein glycosylation. Database URL: www.bgu.ac.il/aglgenes.
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http://dx.doi.org/10.1093/database/bau046 | DOI Listing |
BBA Adv
August 2024
Dept. of Life Sciences, Ben-Gurion University of the Negev, Beersheva, Israel.
While performed by all three domains of life, N-glycosylation in Archaea is less well described than are the parallel eukaryal and bacterial processes. Still, what is known of the archaeal version of this universal post-translational modification reveals numerous seemingly domain-specific traits. Specifically, the biosynthesis of archaeal N-linked glycans relies on distinct pathway steps and components, rare sugars and sugar modifications, as well as unique lipid carriers upon which N-linked glycans are assembled.
View Article and Find Full Text PDFBBA Adv
July 2024
Institute for Extra-cutting-edge Science and Technology Avant-garde Research (X-star), Japan Agency for Marine-Earth Science and Technology (JAMSTEC), 2-15 Natsushima-cho, Yokosuka 273-0061, Japan.
Nat Commun
July 2024
Department of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva, Israel.
The swimming device of archaea-the archaellum-presents asparagine (N)-linked glycans. While N-glycosylation serves numerous roles in archaea, including enabling their survival in extreme environments, how this post-translational modification contributes to cell motility remains under-explored. Here, we report the cryo-EM structure of archaellum filaments from the haloarchaeon Halobacterium salinarum, where archaellins, the building blocks of the archaellum, are N-glycosylated, and the N-glycosylation pathway is well-resolved.
View Article and Find Full Text PDFJ Biosci Bioeng
May 2024
General Research Laboratory, Ozeki Corporation, 4-9 Imazu Dezaike-cho, Nishinomiya, Hyogo 663-8227, Japan.
Hyperthermostable endoglucanases of glycoside hydrolase family 12 from the archaeon Pyrococcus furiosus (EGPf) catalyze the hydrolysis of β-1,4-glucosidic linkages in cellulose and β-glucan structures that contain β-1,3- and β-1,4-mixed linkages. In this study, EGPf was heterologously expressed with Aspergillus niger and the recombinant enzyme was characterized. The successful expression of EGPf resulted as N-glycosylated protein in its secretion into the culture medium.
View Article and Find Full Text PDFEnviron Microbiol Rep
February 2024
College of Food Science and Technology, Shanghai Ocean University, Shanghai, China.
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