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

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RECOMBINANT SMALL HEAT SHOCK PROTEIN FROM ACHOLEPLASMA LAIDLAWII INCREASES THE ESCHERICHIA COLI VIABILITY IN THERMAL STRESS BY SELECTIVE PROTEIN RESCUE

Form of presentation

Articles in international journals and collections

Year of publication

2017

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Authors, employees of KFU

Bogachev Mikhail Igorevich, author

Kayumov Ayrat Rashitovich, author

Other authors

Artamonova T. O., author

Borchsenius S. N., author

Lazarev V. N., author

Manuvera V. A., author

Sabantsev A. V., author

Vishnyakov I. E., author

Bibliographic description in the original language

Kayumov A.R. Recombinant small heat shock protein from Acholeplasma laidlawii increases the Escherichia coli viability in thermal stress by selective protein rescue / A.R. Kayumov, M.I. Bogachev, V.A. Manuvera, V.N. Lazarev, A.V. Sabantsev, T.O. Artamonova, S.N. Borchsenius, I.E. Vishnyakov // Molecular Biology. - 2017. - V.51, Is.1. - P.112-121.

Annotation

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 I

Keywords

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

The name of the journal

Molecular Biology

URL

https://www.scopus.com/inward/record.uri?eid=2-s2.0-85013361003&doi=10.1134%2fS0026893317010083&partnerID=40&md5=647472810d157b81013f2992f0f60baa

Please use this ID to quote from or refer to the card

https://repository.kpfu.ru/eng/?p_id=153801&p_lang=2

Full metadata record

Field DC	Value	Language
dc.contributor.author	Bogachev Mikhail Igorevich	ru_RU
dc.contributor.author	Kayumov Ayrat Rashitovich	ru_RU
dc.contributor.author	Artamonova T. O.	ru_RU
dc.contributor.author	Borchsenius S. N.	ru_RU
dc.contributor.author	Lazarev V. N.	ru_RU
dc.contributor.author	Manuvera V. A.	ru_RU
dc.contributor.author	Sabantsev A. V.	ru_RU
dc.contributor.author	Vishnyakov I. E.	ru_RU
dc.date.accessioned	2017-01-01T00:00:00Z	ru_RU
dc.date.available	2017-01-01T00:00:00Z	ru_RU
dc.date.issued	2017	ru_RU
dc.identifier.citation	Kayumov A.R. Recombinant small heat shock protein from Acholeplasma laidlawii increases the Escherichia coli viability in thermal stress by selective protein rescue / A.R. Kayumov, M.I. Bogachev, V.A. Manuvera, V.N. Lazarev, A.V. Sabantsev, T.O. Artamonova, S.N. Borchsenius, I.E. Vishnyakov // Molecular Biology. - 2017. - V.51, Is.1. - P.112-121.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=153801&p_lang=2	ru_RU
dc.description.abstract	Molecular Biology	ru_RU
dc.description.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 I	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	Acholeplasma laidlawii	ru_RU
dc.subject	mass spectrometry	ru_RU
dc.subject	pull-down assay	ru_RU
dc.subject	small heat shock protein	ru_RU
dc.subject	statistical analysis	ru_RU
dc.subject	target proteins	ru_RU
dc.subject	thermal stability of Escherichia coli	ru_RU
dc.title	Recombinant small heat shock protein from Acholeplasma laidlawii increases the Escherichia coli viability in thermal stress by selective protein rescue	ru_RU
dc.type	Articles in international journals and collections	ru_RU