Glycogen catabolism in <I>Synechococcus elongatus</I> PCC 7942

DOI

Bibliographic Information

Other Title
  • <I>Synechococcus elongatus</I> PCC 7942 におけるグリコーゲン分解代謝

Abstract

Previous analysis of the mutants of Synechococcus elongatus PCC 7942 defective in glycogen biosynthesis indicated that the storage polysaccharide has the significant role for the viability under high-salt and oxidative stresses. In the present study, mutants of phosphorylase (glgP), debranching enzyme (glgX) and α-1,4-glucanotransferase (malQ) have been constructed and characterized for the catabolic activity of glycogen accumulated in the cell.<br>The cellular content of glycogen in wild type (WT) cells remained constant throughout the diurnal cycles (12 h/12 h) of the growth and very little decrease was observed in the dark period. In contrast, the glycogen breakdown was highly stimulated when WT cells were exposed to 0.2 M NaCl in the continuous darkness. Under the same conditions, the activity of glycogen degradation in the glgP, glgX and malQ mutants was markedly reduced as compared to WT. It is therefore concluded that these enzymes are responsible for the glycogen catabolism in cyanobacteria.

Journal

Details 詳細情報について

  • CRID
    1390001205632529152
  • NII Article ID
    130006994268
  • DOI
    10.14841/jspp.2009.0.0295.0
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

Report a problem

Back to top