Carbohydrate metabolism in mutants of the cyanobacterium Synechococcus elongatus PCC 7942 defective in glycogen synthesis.

Abstract:

:ADP-glucose pyrophosphorylase (AGPase) and glycogen synthase (GS) catalyze the first two reactions of glycogen synthesis in cyanobacteria. Mutants defective in each of these enzymes in Synechococcus elongatus PCC 7942 were constructed and characterized. Activities of the corresponding enzymes in the selected mutants were virtually undetectable, and their ability to synthesize glycogen was entirely abolished. The maximal activities of photosynthetic O(2) evolution and the rates of respiration in the dark were significantly decreased in the mutants compared to those in wild-type cells. Addition of 0.2 M NaCl or 3 mM H(2)O(2) to liquid cultures markedly inhibited the growth of the AGPase and GS mutants, while the same treatment had only marginal effects on the wild type. These results suggest a significant role for storage polysaccharides in tolerance to salt or oxidative stress.

journal_name

Appl Environ Microbiol

authors

Suzuki E,Ohkawa H,Moriya K,Matsubara T,Nagaike Y,Iwasaki I,Fujiwara S,Tsuzuki M,Nakamura Y

doi

10.1128/AEM.00397-08

subject

Has Abstract

pub_date

2010-05-01 00:00:00

pages

3153-9

issue

10

eissn

0099-2240

issn

1098-5336

pii

AEM.00397-08

journal_volume

76

pub_type

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