Functional analysis of the two homologous psbA gene copies in Synechocystis PCC 6714 and PCC 6803

1993 ◽  
Vol 21 (2) ◽  
pp. 249-258 ◽  
Author(s):  
A. Bouyoub ◽  
C. Vernotte ◽  
C. Astier
1990 ◽  
Vol 45 (5) ◽  
pp. 436-440 ◽  
Author(s):  
S. Creuzet ◽  
G. Ajlani ◽  
C. Vernotte ◽  
C. Astier

A new Synechocystis 6714 mutant, loxIIA, resistant to the phenol-type herbicide ioxynil was isolated and characterized. The mutation found in the psbA gene (encoding the D1 photosystem II protein) is at the same codon 266 as for the first ioxynil-resistant mutant IoxIA previously selected [G. Ajlani. I. Meyer, C. Vernotte. and C. Astier, FEBS Lett. 246, 207-210 (1989)]. In IoxIIA, the change of Asn 266 to Asp gives a 3 × resistance, whereas in IoxIA, the change of the same amino acid to Thr gives a 10 × resistance. The effect of these different amino acid substitutions on the ioxynil resistance phenotype has allowed us to construct molecular models and calculate the hydrogen-bonding energies between the hydroxyl group of ioxynil and the respective amino acids at position 266.


Author(s):  
Péter B. Kós ◽  
Zsuzsanna Deák ◽  
Otilia Cheregi ◽  
Imre Vass
Keyword(s):  

Microbiology ◽  
2014 ◽  
Vol 160 (1) ◽  
pp. 228-241 ◽  
Author(s):  
Wen-Ting Ke ◽  
Guo-Zheng Dai ◽  
Hai-Bo Jiang ◽  
Rui Zhang ◽  
Bao-Sheng Qiu

Synechocystis sp. PCC 6803 possesses only one sod gene, sodB, encoding iron superoxide dismutase (FeSOD). It could not be knocked out completely by direct insertion of the kanamycin resistance cassette. When the promoter of sodB in WT Synechocystis was replaced with the copper-regulated promoter PpetE, a completely segregated PpetE–sodB strain could be obtained. When this strain was cultured in copper-starved BG11 medium, the chlorophyll a content was greatly reduced, growth was seriously inhibited and the strain was nearly dead during the 8 days of growth, whilst the WT strain grew well under the same growth conditions. These results indicated that sodB was essential for photoautotrophic growth of Synechocystis. The reduction of sodB gene copies in the Synechocystis genome rendered the cells more sensitive to oxidative stress produced by methyl viologen and norflurazon. sodB still could not be knocked out completely after active expression of sodC (encoding Cu/ZnSOD) from Synechococcus sp. CC9311 in the neutral site slr0168 under the control of the psbAII promoter, which means the function of FeSOD could not be complemented completely by Cu/ZnSOD. Heterogeneously expressed sodC increased the oxidation and photoinhibition tolerance of the Synechocystis sodB knockdown mutant. Membrane fractionation followed by immunoblotting revealed that FeSOD was localized in the cytoplasm, and Cu/ZnSOD was localized in the soluble and thylakoid membrane fractions of the transformed Synechocystis. Cu/ZnSOD has a predicted N-terminal signal peptide, so it is probably a lumen protein. The different subcellular localization of these two SODs may have resulted in the failure of substitution of sodC for sodB.


FEBS Letters ◽  
2002 ◽  
Vol 517 (1-3) ◽  
pp. 50-54 ◽  
Author(s):  
Fernando P Molina-Heredia ◽  
Alexis Balme ◽  
Manuel Hervás ◽  
José A Navarro ◽  
Miguel A De la Rosa
Keyword(s):  

2013 ◽  
Vol 55 (4) ◽  
pp. 371-376 ◽  
Author(s):  
Yeong Byeon ◽  
Kyungjin Lee ◽  
Youn-Il Park ◽  
Sangkyu Park ◽  
Kyoungwhan Back

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