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 Microbioljournal_title
Applied and environmental microbiologyauthors
Suzuki E,Ohkawa H,Moriya K,Matsubara T,Nagaike Y,Iwasaki I,Fujiwara S,Tsuzuki M,Nakamura Ydoi
10.1128/AEM.00397-08subject
Has Abstractpub_date
2010-05-01 00:00:00pages
3153-9issue
10eissn
0099-2240issn
1098-5336pii
AEM.00397-08journal_volume
76pub_type
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