title: [Recombinant small heat shock protein from Acholeplasma laidlawii increases the Escherichia coli viability in thermal stress by selective protein rescue].
abstract: 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.
authors.affiliation: Kazan Federal University, Kazan, 420008 Russia.
authors.forename: A R
authors.initials: AR
authors.lastname: Kayumov
authors.affiliation: LETI St. Petersburg State Electrotechnical University, St. Petersburg, 197376 Russia.
authors.forename: M I
authors.initials: MI
authors.lastname: Bogachev
authors.affiliation: Institute of Physico-Chemical Medicine, Federal Medical-Biological Agency of Russia, Moscow, 119992 Russia.
authors.forename: V A
authors.initials: VA
authors.lastname: Manuvera
authors.affiliation: Institute of Physico-Chemical Medicine, Federal Medical-Biological Agency of Russia, Moscow, 119992 Russia.
authors.forename: V N
authors.initials: VN
authors.lastname: Lazarev
authors.affiliation: Peter the Great St. Petersburg Polytechnic University, St. Petersburg, 195251 Russia.
authors.forename: A V
authors.initials: AV
authors.lastname: Sabantsev
authors.affiliation: Peter the Great St. Petersburg Polytechnic University, St. Petersburg, 195251 Russia.
authors.forename: T O
authors.initials: TO
authors.lastname: Artamonova
authors.affiliation: Institute of Cytology, Russian Academy of Sciences, St. Petersburg, 194064 Russia.
authors.forename: S N
authors.initials: SN
authors.lastname: Borchsenius
authors.affiliation: Peter the Great St. Petersburg Polytechnic University, St. Petersburg, 195251 Russia.|Institute of Cytology, Russian Academy of Sciences, St. Petersburg, 194064 Russia.|innvish@gmail.com.
authors.forename: I E
authors.initials: IE
authors.lastname: Vishnyakov
mesh_terms: D000128:Acholeplasma laidlawii / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000502:physiology*; D050888:Heat-Shock Proteins, Small / Q000737:chemistry*; D006358:Hot Temperature; D011994:Recombinant Proteins / Q000737:chemistry; D013312:Stress, Physiological
chemical_list: D001426:Bacterial Proteins; D050888:Heat-Shock Proteins, Small; D011994:Recombinant Proteins
keywords: Acholeplasma laidlawii; mass spectrometry; pull-down assay; small heat shock protein; statistical analysis; target proteins; thermal stability of Escherichia coli