Anomalous dissociative behavior of the major glycosylated component of the cellulosome of clostridium thermocellum

Ely Morgenstern, Edward A. Bayer, Raphael Lamed

Research output: Contribution to journalArticlepeer-review

Abstract

The cellulosome of Clostridium thermocellum is a highly cohesive multienzyme complex that is capable of completely solubilizing insoluble cellulose. One of the major cellulosomal components, the glycosylated S1 subunit, is believed to play an important structural role and normally migrates in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an Mr of 210,000. It is shown here that by simply altering the conditions (pH or ionic strength) of the environment prior to electrophoresis, a different migratory profile for S1 emerges, yielding a collection of bands, all of which migrate faster than the parent band. The original electrophoretic behavior of S1 can be reproduced on restoration of the original pH and ionic strength. These results may bear important significance for the physiological role of the S1 subunit in facilitating the observed synergistic action of the other (cellulolytic) components of the cellulosome.

Original languageEnglish
Pages (from-to)129-136
Number of pages8
JournalApplied Biochemistry and Biotechnology
Volume30
Issue number2
DOIs
StatePublished - Aug 1991

Keywords

  • Cellulosome
  • Clostridium thermocellum
  • SDS-PAGE, anamolous migration
  • cellulase
  • multienzyme complex
  • subunit dissociation

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