|
Translations of Published Articles
Bacterial nucleoid protein Dps binds structured RNA molecules
A. A. Bykovab, K. S. Shavkunovac, V. V. Panyukovdc, O. N. Ozolineac a 1142290, Institute of Cell Biophysics of Russian Academy of Sciences, Pushchino, Moscow region, Russia
b 2142290, Pushchino State Institute of Natural Sciences, Pushchino, Moscow region, Russia
c 142290, Pushchino Scientific Center of Russian Academy of Sciences, Pushchino, Moscow region, Russia
d 142290, Institute of Mathematical Problems of Biology — the Branch of Keldysh Institute of Applied Mathematics of Russian Academy of Sciences, Pushchino, Moscow region, Russia
Abstract:
Architectural protein Dps of bacterial nucleoid employs side lysine
groups at its N-terminal modules for interacting with the sugar-phosphate backbone
of the DNA. Electrostatic nature of interaction assumes the potential ability of Dps
to bind with any nucleotide sequence, including RNA. The available data also
indicate that Dps exhibits enhanced affinity to branched DNA structures. In RNA
molecules such structures are formed more frequently than in DNA. Hence, the aim
of this investigation was to study the ability of purified Dps immobilized on
acrylate spheres to bind short RNAs isolated from bacterial cells. It appeared that
transport and small regulatory RNAs forming stable secondary structures are the
preferred targets for such interaction. Among RNAs identified in complexes with
Dps 8 transcripts corresponded to intergenic spaces, which might indicate the
presence of novel genes. Moreover, 9–13 nucleotide long products, belonging to
small untranslated RNAs SdsR and RyeA and transcribed from both strands of the
same locus, were registered. Since the amount of longer transcripts from this region
was at least five-fold lower, it can be presumed that pairs of counter-synthesized
products form partly complementary duplexes subjected to the controlled
processing. The selectivity of Dps to these molecules, as well as to other structured
RNAs, indicates a possibility of its involvement not only in bacterial genome
condensation, but also in maintaining the functional state of the transcriptome.
Key words:
Dps, Dps-RNA complexes, pull-down assay, RNA-seq.
Received 19.01.2017, Published 24.01.2017
Citation:
A. A. Bykov, K. S. Shavkunov, V. V. Panyukov, O. N. Ozoline, “Bacterial nucleoid protein Dps binds structured RNA molecules”, Mat. Biolog. Bioinform., 12, Suppl. (2017), t1–t11
Linking options:
https://www.mathnet.ru/eng/mbb314 https://www.mathnet.ru/eng/mbb/v12/i3/p1
|
Statistics & downloads: |
Abstract page: | 184 | Full-text PDF : | 172 | References: | 27 |
|