Biology Reference
In-Depth Information
In the past few years, significant progress has been made in the identi-
fication of ROS-scavenging and detoxification processes in cyanobacteria,
unravelling the crucial and pleiotropic role of glutathione and glutathione-
dependent enzymes, such as the glutaredoxin (Grxs) enzymes, which con-
trol the redox state of cellular thiols; the glyoxalases (Glxs), which detoxify
the toxic metabolite methylglyoxal; and the glutathione transferases (GSTs),
which detoxify many xenobiotics. The selectivity-redundancy of these
enzyme families need to be thoroughly investigated to determine what
range of oxidants (GSTs) or oxidized proteins (Grxs) they can detoxify
(Gsts) or repair (Grxs), and in which subcellular compartment they act.
Another important challenge in the near future will be to analyse how
redox regulation of proteins by glutathionylation and deglutathionylation
via the Grxs enzymes affects global gene expression and metabolism in cells
growing in various environmental conditions or facing oxidative challenges.
These studies will be facilitated by the recent breakthroughs in genome
sequencing and comparative genomics, which enable genome-based recon-
struction of an organism's metabolism, as well as the powerful genetics of
various model strains. Indeed, the bioinformatic method of “prediction by
analogy” has its limits. Until we do the experiments, we may mispredict the
real function or properties of a gene product ( Bender, 2011 ; Domain et al.,
2004 ; Figge et al., 2001 ).
ACKNOWLEDGEMENTS
Owing to space limitations, it was not possible to cite all research papers relevant to the
presented subject. We sincerely apologize to those authors whose work we could not include.
REFERENCES
Abed, R. M., Dobretsov, S., & Sudesh, K. (2009). Applications of cyanobacteria in biotech-
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Allocati, N., Federici, L., Masulli, M., & Di Ilio, C. (2009). Glutathione transferases in bacteria.
The FEBS Journal , 276 , 58-75.
Archibald, J. M. (2009). The puzzle of plastid evolution. Current Biology: CB , 19 , R81-R88.
Ashida, H., Sawa, Y., & Shibata, H. (2005). Cloning, biochemical and phylogenetic
characterizations of gamma-glutamylcysteine synthetase from Anabaena sp. PCC 7120.
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Battchikova, N.,Vainonen, J. P.,Vorontsova, N., Keranen, M., Carmel, D., & Aro, E. M. (2010).
Dynamic changes in the proteome of Synechocystis 6803 in response to CO(2) limitation
revealed by quantitative proteomics. Journal of Proteome Research , 9 , 5896-5912.
Bender, R. A. (2011). The danger of annotation by analogy: most “thiI” genes play no role in
thiamine biosynthesis. Journal of Bacteriology , 193 , 4574-4575.
Beria, B. M., & Pakrasi, H. B. (2012). Up-regulation of plasmid-encoded genes during
stationary phase in Synechocystis sp. PCC 6803, a cyanobacterium. Applied and Environ-
mental Microbiology .
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