Sequence-based protein stabilization in the absence of glycosylation

Tan, Nikki Y., Bailey, Ulla-Maja, Jamaluddin, M Fairuz, Mahmud, S Halimah Binte, Raman, Suresh C. and Schulz, Benjamin L. (2014) Sequence-based protein stabilization in the absence of glycosylation. Nature Communications, 5 3099: 1-7. doi:10.1038/ncomms4099

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Author Tan, Nikki Y.
Bailey, Ulla-Maja
Jamaluddin, M Fairuz
Mahmud, S Halimah Binte
Raman, Suresh C.
Schulz, Benjamin L.
Title Sequence-based protein stabilization in the absence of glycosylation
Journal name Nature Communications   Check publisher's open access policy
ISSN 2041-1723
Publication date 2014-01-17
Sub-type Article (original research)
DOI 10.1038/ncomms4099
Open Access Status File (Publisher version)
Volume 5
Issue 3099
Start page 1
End page 7
Total pages 7
Place of publication London, United Kingdom
Publisher Nature Publishing Group
Language eng
Formatted abstract
Asparagine-linked N-glycosylation is a common modification of proteins that promotes productive protein folding and increases protein stability. Although N-glycosylation is important for glycoprotein folding, the precise sites of glycosylation are often not conserved between protein homologues. Here we show that, in Saccharomyces cerevisiae, proteins upregulated during sporulation under nutrient deprivation have few N-glycosylation sequons and in their place tend to contain clusters of like-charged amino-acid residues. Incorporation of such sequences complements loss of in vivo protein function in the absence of glycosylation. Targeted point mutation to create such sequence stretches at glycosylation sequons in model glycoproteins increases in vitro protein stability and activity. A dependence on glycosylation for protein stability or activity can therefore be rescued with a small number of local point mutations, providing evolutionary flexibility in the precise location of N-glycans, allowing protein expression under nutrient-limiting conditions, and improving recombinant protein production.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
School of Chemistry and Molecular Biosciences
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Citation counts: TR Web of Science Citation Count  Cited 8 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 8 times in Scopus Article | Citations
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Created: Fri, 14 Feb 2014, 20:19:17 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences