Abstract
Ever since the discovery of the first glycosylated archaeal protein, namely the Halobacterium salinarum surface-layer glycoprotein some 35 years ago, research on haloarchaea has been at the forefront of efforts to decipher the archaeal version of N-glycosylation, a universal post-translational modification. Now, with the availability of sufficient numbers of genome sequences and the development of appropriate experimental tools, the possibility for detailed molecular analysis of archaeal N-glycosylation pathways is being realized, using haloarchaeal species as model systems. In this chapter, current understanding of N-glycosylation in Archaea and the contribution of studies on Haloferax volcanii to such endeavors are described.
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Acknowledgments
Research in the Eichler laboratory is supported by the Israel Science Foundation (grant 30/07). S.Y.-D. is the recipient of a Negev-Faran Associates Scholarship, while L.K. is the recipient of a Negev-Zin Associates Scholarship.
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Eichler, J. et al. (2011). Salty and Sweet: Protein Glycosylation in Haloferax volcanii . In: Ventosa, A., Oren, A., Ma, Y. (eds) Halophiles and Hypersaline Environments. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-20198-1_12
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DOI: https://doi.org/10.1007/978-3-642-20198-1_12
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