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AMYLOIDOGENIC PROPERTIES OF ARCHEAL PROTEINS DEPEND ON
ENVIRONMENTAL CONDITIONS
Kirill S. Antonets, Polina B. Drozdova, Anton A. Nizhnikov
St.Petersburg State University
St.Petersburg Branch of Vavilov Institute of General Genetics, RAS, St. Petersburg
Russia
Amyloids are fibrillary protein aggregates possessing cross-beta structure. These
aggregates are highly resistant to different environmental factors. That is why it is an
interesting question, whether extreme habitats of some prokaryotes and amyloidogenic
properties of their proteins are connected? To answer this question, we analyzed
proteomes of 76 archaeal and 104 bacterial species. The fraction of amyloidogenic
proteins in proteomes of acidophilic, thermophilic and hyperthermophilic archeae was
shown to be significantly increased in comparison with neutrophilic and mesophilic
species. It is interesting to note, that the fraction of such proteins of halophilic archeae
was decreased, and we did not notice similar patterns in bacterial proteomes. Next, we
analyzed distribution of amyloidogeneic proteins among different functional classes.
We have shown that amyloidogenic proteins tend to be in the relatively big functional
groups, and identified the groups, proteins of which tend to become amyloidogenic at
extreme conditions. Proteins, connected with dynamics and structure of chromatin,
appeared to be more influenced by environmental conditions. Taken together, in the
current work the dependence of amyloidogenic properties on habitual conditions was
first shown.
The study was supported by RFBR (Project 14-04-31838) and by the grant of the
President of the Russian Federation № MK-4854.2015.4.