Skip to main content

Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans.

Publication ,  Journal Article
Cohen-Rosenzweig, C; Guan, Z; Shaanan, B; Eichler, J
Published in: Appl Environ Microbiol
January 2014

Across evolution, N-glycosylation involves oligosaccharyltransferases that transfer lipid-linked glycans to selected Asn residues of target proteins. While these enzymes catalyze similar reactions in each domain, differences exist in terms of the chemical composition, length and degree of phosphorylation of the lipid glycan carrier, the sugar linking the glycan to the lipid carrier, and the composition and structure of the transferred glycan. To gain insight into how oligosaccharyltransferases cope with such substrate diversity, the present study analyzed the archaeal oligosaccharyltransferase AglB from four haloarchaeal species. Accordingly, it was shown that despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei could readily replace their counterpart from Haloferax volcanii when introduced into Hfx. volcanii cells deleted of aglB. As the four enzymes show significant sequence and apparently structural homology, it appears that the functional similarity of the four AglB proteins reflects the relaxed substrate specificity of these enzymes. Such demonstration of AglB substrate promiscuity is important not only for better understanding of N-glycosylation in Archaea and elsewhere but also for efforts aimed at transforming Hfx. volcanii into a glycoengineering platform.

Duke Scholars

Published In

Appl Environ Microbiol

DOI

EISSN

1098-5336

Publication Date

January 2014

Volume

80

Issue

2

Start / End Page

486 / 496

Location

United States

Related Subject Headings

  • Substrate Specificity
  • Protein Conformation
  • Polysaccharides
  • Molecular Sequence Data
  • Models, Molecular
  • Microbiology
  • Membrane Proteins
  • Hexosyltransferases
  • Haloferax volcanii
  • Halobacterium salinarum
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Cohen-Rosenzweig, C., Guan, Z., Shaanan, B., & Eichler, J. (2014). Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans. Appl Environ Microbiol, 80(2), 486–496. https://doi.org/10.1128/AEM.03191-13
Cohen-Rosenzweig, Chen, Ziqiang Guan, Boaz Shaanan, and Jerry Eichler. “Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans.Appl Environ Microbiol 80, no. 2 (January 2014): 486–96. https://doi.org/10.1128/AEM.03191-13.
Cohen-Rosenzweig C, Guan Z, Shaanan B, Eichler J. Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans. Appl Environ Microbiol. 2014 Jan;80(2):486–96.
Cohen-Rosenzweig, Chen, et al. “Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans.Appl Environ Microbiol, vol. 80, no. 2, Jan. 2014, pp. 486–96. Pubmed, doi:10.1128/AEM.03191-13.
Cohen-Rosenzweig C, Guan Z, Shaanan B, Eichler J. Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans. Appl Environ Microbiol. 2014 Jan;80(2):486–496.

Published In

Appl Environ Microbiol

DOI

EISSN

1098-5336

Publication Date

January 2014

Volume

80

Issue

2

Start / End Page

486 / 496

Location

United States

Related Subject Headings

  • Substrate Specificity
  • Protein Conformation
  • Polysaccharides
  • Molecular Sequence Data
  • Models, Molecular
  • Microbiology
  • Membrane Proteins
  • Hexosyltransferases
  • Haloferax volcanii
  • Halobacterium salinarum