Halophilic archaea use a fusion-based mating system for lateral gene transfer across cells, yet the molecular mechanisms involved remain unknown. Previous work implied that cell fusion involves cell–cell recognition since fusion occurs more efficiently between cells from the same species. Long believed to be restricted only to Eukarya, it is now known that cells of all three domains of life perform N-glycosylation, the covalent attachment of glycans to select target asparagine residues in proteins, and that this post-translational modification is common for archaeal cell surface proteins. Here, we show that differences in glycosylation of the Haloferax volcanii surface-layer glycoprotein, brought about either by changing medium salinity or by knocking out key glycosylation genes, reduced mating success. Thus, different glycosylation patterns are likely to underlie mating preference in halophilic archaea, contributing to speciation processes.
Cell Surface Glycosylation Is Required for Efficient Mating of Haloferax volcanii
Yarden Shalev,Israela Turgeman-Grott,A. Tamir,J. Eichler,U. Gophna
Published 2017 in Frontiers in Microbiology
ABSTRACT
PUBLICATION RECORD
- Publication year
2017
- Venue
Frontiers in Microbiology
- Publication date
2017-07-05
- Fields of study
Biology, Medicine, Environmental Science
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
CITATION MAP
EXTRACTION MAP
CLAIMS
- No claims are published for this paper.
CONCEPTS
- No concepts are published for this paper.
REFERENCES
Showing 1-28 of 28 references · Page 1 of 1
CITED BY
Showing 1-41 of 41 citing papers · Page 1 of 1