Salty and Sweet: Protein Glycosylation in Haloferax volcanii

Jerry Eichler; Doron Calo; Lina Kaminski; Lina Kandiba; Zvia Konrad; Hilla Magidovich; Shai Naparstek; Sophie Yurist-Doutsch

doi:10.1007/978-3-642-20198-1_12

Salty and Sweet: Protein Glycosylation in Haloferax volcanii

Jerry Eichler, Doron Calo, Lina Kaminski, Lina Kandiba, Zvia Konrad, Hilla Magidovich, Shai Naparstek, Sophie Yurist-Doutsch

Department of Life Sciences

Ben-Gurion University of the Negev

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

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.

Original language	American English
Title of host publication	Halophiles and Hypersaline Environments
Editors	A. Ventosa, A. Oren
Publisher	Springer Berlin
Pages	227-235
Number of pages	9
ISBN (Electronic)	978-3-642-20198-1
ISBN (Print)	978-3-642-20197-4
DOIs	https://doi.org/10.1007/978-3-642-20198-1_12
State	Published - 27 May 2011

Keywords

Halobacterium salinarum
Halophilic Archaea
Hexuronic Acid
Protein Glycosylation
Sulfated Polysaccharide

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10.1007/978-3-642-20198-1_12

Cite this

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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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T2 - Protein Glycosylation in Haloferax volcanii

AU - Eichler, Jerry

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AU - Kaminski, Lina

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AU - Konrad, Zvia

AU - Magidovich, Hilla

AU - Naparstek, Shai

AU - Yurist-Doutsch, Sophie

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AB - 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.

KW - Halobacterium salinarum

KW - Halophilic Archaea

KW - Hexuronic Acid

KW - Protein Glycosylation

KW - Sulfated Polysaccharide

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A2 - Oren, A.

PB - Springer Berlin

ER -

Salty and Sweet: Protein Glycosylation in Haloferax volcanii

Abstract

Keywords

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