Deletion of a Single Glycosyltransferase in Caldicellulosiruptor bescii Eliminates Protein Glycosylation and Growth on Crystalline Cellulose

Michael Himmel, Yannick Bomble, Jordan Russell, Sun-Ki Kim, Justin Duma, Harald Nothaft, Christine Szymanski, Janet Westpheling

Research output: Contribution to journalArticlepeer-review

9 Scopus Citations

Abstract

Protein glycosylation pathways have been identified in a variety of bacteria and are best understood in pathogens and commensals in which the glycosylation targets are cell surface proteins, such as S layers, pili, and flagella. In contrast, very little is known about the glycosylation of bacterial enzymes, especially those secreted by cellulolytic bacteria. Caldicellulosiruptor bescii secretes several unique synergistic multifunctional biomass-degrading enzymes, notably cellulase A which is largely responsible for this organism's ability to grow on lignocellulosic biomass without the conventional pretreatment. It was recently discovered that extracellular CelA is heavily glycosylated. In this work, we identified an O-glycosyltransferase in the C. bescii chromosome and targeted it for deletion. The resulting mutant was unable to grow on crystalline cellulose and showed no detectable protein glycosylation. Multifunctional biomass-degrading enzymes in this strain were rapidly degraded. With the genetic tools available in C. bescii, this system represents a unique opportunity to study the role of bacterial enzyme glycosylation as well an investigation of the pathway for protein glycosylation in a non-pathogen.

Original languageAmerican English
Article number259
Number of pages10
JournalBiotechnology for Biofuels
Volume11
Issue number1
DOIs
StatePublished - 2018

Bibliographical note

Publisher Copyright:
© 2018 The Author(s).

NREL Publication Number

  • NREL/JA-2700-72558

Keywords

  • bacterial enzymes
  • glycosylation
  • lignocellulosic biomass

Fingerprint

Dive into the research topics of 'Deletion of a Single Glycosyltransferase in Caldicellulosiruptor bescii Eliminates Protein Glycosylation and Growth on Crystalline Cellulose'. Together they form a unique fingerprint.

Cite this