Literature DB >> 35974488

Superoxide dismutase activity in the cyanobacterium Microcystis aeruginosa after surface bloom formation.

Antonella Canini1, Donatella Leonardi1, Maria Grilli Caiola1.   

Abstract

•  The presence of superoxide dismutase (SOD) enzymes and the response of SOD after in vitro induction and decay of a surface bloom are shown in cultures of the cyanobacterium Microcystis aeruginosa. •  The SOD enzymes of surface blooms, early degenerate and completely degenerate cultures were assayed by staining for SOD activity, immunoblotting and immunogold labelling. •  One band of Mn- and three bands of Fe-SOD were detected in cell extracts. During surface bloom formation, Fe-SOD activity increased fivefold compared with that in control cells; no variation was detected in Mn-SOD activity. However, in early degenerate cultures, Fe-SOD activity decreased to that seen in control cultures, while activity disappeared in completely degenerate cultures. Immunogold labelling showed that Fe-SOD was localized in the cytoplasmic and thylakoid membranes of Microcystis. The extent of labelling paralleled the course of Fe-SOD activity with an increase in particles in surface blooming cells. •  The results suggest Fe-SOD increased due to photooxidative stress. However, under prolonged photooxidative stress, high concentrations of active oxygen species could directly, or indirectly, inactivate and degrade Fe-SOD.

Entities:  

Keywords:  Microcystis aeruginosa; immunogold labelling; photooxidation; photosynthesis; superoxide dismutase (SOD)

Year:  2001        PMID: 35974488     DOI: 10.1046/j.0028-646x.2001.00244.x

Source DB:  PubMed          Journal:  New Phytol        ISSN: 0028-646X            Impact factor:   10.323


  11 in total

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Authors:  K Asada; K Yoshikawa; M Takahashi; Y Maeda; K Enmanji
Journal:  J Biol Chem       Date:  1975-04-25       Impact factor: 5.157

2.  Purification and characterization of a homodimeric catalase-peroxidase from the cyanobacterium Anacystis nidulans.

Authors:  C Obinger; G Regelsberger; G Strasser; U Burner; G A Peschek
Journal:  Biochem Biophys Res Commun       Date:  1997-06-27       Impact factor: 3.575

3.  Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation.

Authors:  D C Salo; R E Pacifici; S W Lin; C Giulivi; K J Davies
Journal:  J Biol Chem       Date:  1990-07-15       Impact factor: 5.157

4.  Inactivation and degradation of CuZn-SOD by active oxygen species in wheat chloroplasts exposed to photooxidative stress.

Authors:  L M Casano; L D Gómez; H R Lascano; C A González; V S Trippi
Journal:  Plant Cell Physiol       Date:  1997-04       Impact factor: 4.927

Review 5.  Biochemistry of oxygen toxicity.

Authors:  E Cadenas
Journal:  Annu Rev Biochem       Date:  1989       Impact factor: 23.643

6.  Enzymatic defenses against the toxicity of oxygen and of streptonigrin in Escherichia coli.

Authors:  H M Hassan; I Fridovich
Journal:  J Bacteriol       Date:  1977-03       Impact factor: 3.490

7.  The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.

Authors:  K Weber; M Osborn
Journal:  J Biol Chem       Date:  1969-08-25       Impact factor: 5.157

8.  Photooxidative death in blue-green algae.

Authors:  A Abeliovich; M Shilo
Journal:  J Bacteriol       Date:  1972-09       Impact factor: 3.490

9.  Purification and characterization of a hydroperoxidase from the cyanobacterium Synechocystis PCC 6803: identification of its gene by peptide mass mapping using matrix assisted laser desorption ionization time-of-flight mass spectrometry.

Authors:  G Regelsberger; C Obinger; R Zoder; F Altmann; G A Peschek
Journal:  FEMS Microbiol Lett       Date:  1999-01-01       Impact factor: 2.742

10.  Characterization of four superoxide dismutase genes from a filamentous cyanobacterium.

Authors:  W S Campbell; D E Laudenbach
Journal:  J Bacteriol       Date:  1995-02       Impact factor: 3.490

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