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Updated: Apr 28, 2026

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
aglgenes, A curated and searchable database of archaeal N-glycosylation pathway components
1Department of Life Sciences, Ben Gurion University of the Negev, P.O. Box 653, Beersheva 84105, Israel.
Abstract:
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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