Viral genomes can encode for many proteins do not directly
promote virus production but can modify the functionality of the cells they
infect to aid the virus indirectly. A good example of this is cyanophages which
code for multiple proteins used in cyanobacteria photosynthesis, indirectly
promoting phage reproduction. This study reports, for the first time, how giant
viruses code for proteorhodopsins. Five viral proteins were of particular
interest in this study which show similarity to previously studied bacterial
proteorhodopsins.
Yutin and Koonin (2012) compared rhodopsin
proteins across viral, archaeal, bacterial, and eukaryotic sequences, by aligning
them and comparing for similar sequences. This showed the viral proteins to
have high conservation, with 7 transmembrane helicases being especially
conserved.
The viral proteins were also shown to
have the presence of invariant lysine and aspartic acid in the viral sequences
which suggests retinal binding and proton donation would be coded for by the
viruses. However, there was no conservation of the carboxylate proton donor,
characteristic of the light dependent reaction, suggesting that the viral
proteorhodopsins are thought to be used in sensory rather than light dependant
proton pumping. More work would be needed to confirm this function of the
proteins and the reactions they are used in. There would also need to be more
work into the source of the proteins as it is possible that there was masking
in the environmental samples, it could be that the proteins may have been a
product of unclassified rhodopsin genes from protist viral hosts.
The phylogenetic tree analysis showed early acquisition of
the supposed proteorhodopsin genes from either proteorhodopsin coding bacteria
or eukaryotes at the base of the tree. It is thought this would be acquired
through horizontal gene transfer.
The role of proteorhodopsins in unicellular organisms is assumed
to be that they are used as light driven reaction pumps, especially in
oligotrophic environmental conditions. It has also been hypothesised that the rhodopsins
are used in signalling and phototaxis of the organism.
The study has focused overall on the environmental presence
of rhodopsin proteins. For this work to progress the proteins would need to be
isolate from individual organisms to determine the sources of these rhodopsins
and work out their function in the unicellular organism.
Yutin, N., & Koonin, E. V. (2012). Proteorhodopsin
genes in giant viruses. Biology direct,
7, 1, 34.
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