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Vol 51(2017) N 1 p. 112-121; DOI 10.1134/S0026893317010083 Full Text

A.R. Kayumov1, M.I. Bogachev2, V.A. Manuvera3, V.N. Lazarev3, A.V. Sabantsev4, T.O. Artamonova4, S.N. Borchsenius5, I.E. Vishnyakov4,5*

Recombinant small heat shock protein from Acholeplasma laidlawii increases the Escherichia coli viability in thermal stress by selective protein rescue

1Kazan Federal University, Kazan, 420008 Russia
2LETI St. Petersburg State Electrotechnical University, St. Petersburg, 197376 Russia
3Institute of Physico-Chemical Medicine, Federal Medical-Biological Agency of Russia, Moscow, 119992 Russia
4Peter the Great St. Petersburg Polytechnic University, St. Petersburg, 195251 Russia
5Institute of Cytology, Russian Academy of Sciences, St. Petersburg, 194064 Russia

*innvish@gmail.com
Received - 2016-02-27; Accepted - 2016-03-14

In both prokaryotes and eukaryotes, the survival at temperatures considerably exceeding the optimum is supported by intense synthesis of the so-called heat shock proteins (HSPs), which act to overcome the adverse effects of heat stress. Among mycoplasmas (class Mollicutes), which have significantly reduced genomes, only some members of the Acholeplasmataceae family possess small HSPs of the α-crystallin type. Overproduction of a recombinant HSP IbpA (Hsp20) from the free-living mycoplasma Acholeplasma laidlawii was shown to increase the resistance of Escherichia coli to short-term heat shock. It has been long assumed that IbpA prevents protein aggregation and precipitation thereby increasing viability of E. coli cells. Several potential target proteins interacting with IbpA under heat stress were identified, including biosynthetic enzymes, enzymes of energy metabolism, and components of the protein synthesis machinery. Statistical analysis of physicochemical properties indicated that IbpA interaction partners significantly differ in molecular weight, charge, and isoelectric point from other members of the E. coli proteome. Upon shortterm exposure to increased temperature, IbpA was found to preferentially interact with high-molecular weight proteins having a pI of about 5.1, significantly lower than the typical values of E. coli proteins.

small heat shock protein, Acholeplasma laidlawii, pull-down assay, mass spectrometry, statistical analysis, thermal stability of Escherichia coli, target proteins



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