Unorthodox intrasubunit interactions in the cellulosome of Clostridium thermocellum - Identification of structural transitions induced in the S1 subunit

Ely Morag*, Edward A. Bayer, Raphael Lamed

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

Clostridium thermocellum, an anaerobic thermophilic cellulolytic bacterium, produces an extremely cohesive, very high-molecular-mass multicellulase-containing complex termed the cellulosome. One of its components, the S1 subunit, is a nonenzymatic, 210 kDa glycopolypeptide. Upon preconditioning of the intact cellulosome with lowionic-strength or low-pH solutions, the S1 subunit separates in hot sodium dodecyl sulfate (SDS) solutions into a series of defined lowermolecular-mass subcomponents. Under the same conditions, the purified S1 subunit demonstrated the same behavior. Higher levels of glycosylation associated with the larger S1 subcomponents. The data support alterations in the conformational state of the S1 structure that lead to its disintegration induced by combined treatments with SDS and heating. Evidence is provided that this phenomenon may reflect a physiological response of the cellulosome, since similar alterations in S1 appear to accompany its binding to cellulose.

Original languageEnglish
Pages (from-to)205-217
Number of pages13
JournalApplied Biochemistry and Biotechnology
Volume33
Issue number3
DOIs
StatePublished - Jun 1992

Keywords

  • Clostridium thermocellum
  • SDS-PAGE
  • Subunit dissociation
  • anomalous migration
  • cellulose degradation
  • cellulosome
  • conformational transitions
  • multienzyme complex

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