Accumulation of exoglucanase activity in yeast secretory mutants blocked at the endoplasmic reticulum level

FEBS Lett. 1986 Feb 17;196(2):291-5. doi: 10.1016/0014-5793(86)80265-4.

Abstract

Saccharomyces cerevisiae HMSF-176 (sec 18), a thermosensitive secretory mutant blocked at the endoplasmic reticulum (ER) level, drastically increased its osmotic sensitivity when grown at the restrictive temperature of 37 degrees C in high glucose concentration. This fact led to the erroneous interpretation that glucanases were inactive when localized in the ER. The development of a suitable osmotic stabilizer now indicates that sec 18 accumulates exoglucanase activity. Another ER-blocked mutant behaved in a similar way. All the accumulated exoglucanase was found in a soluble form. By contrast, a significant portion of the accumulated invertase remained in a membrane-bound form.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Endoplasmic Reticulum / enzymology
  • Glucosidases / metabolism*
  • Glycoside Hydrolases / metabolism
  • Mutation
  • Osmosis
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics*
  • Solubility
  • Temperature
  • beta-Fructofuranosidase
  • beta-Glucosidase / genetics
  • beta-Glucosidase / metabolism*

Substances

  • Glucosidases
  • Glycoside Hydrolases
  • beta-Glucosidase
  • beta-Fructofuranosidase