КФУ. Карточка публикации. 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

Форма представления

Статьи в зарубежных журналах и сборниках

Год публикации

2017

Язык

английский

Авторы, сотрудники КФУ

Богачев Михаил Игоревич, автор

Каюмов Айрат Рашитович, автор

Другие авторы

Artamonova T. O., автор

Borchsenius S. N., автор

Lazarev V. N., автор

Manuvera V. A., автор

Sabantsev A. V., автор

Vishnyakov I. E., автор

Библиографическое описание на языке оригинала

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.

Аннотация

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

Ключевые слова

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

Название журнала

Molecular Biology

URL

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

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https://repository.kpfu.ru/?p_id=153801

Полная запись метаданных

Поле DC	Значение	Язык
dc.contributor.author	Богачев Михаил Игоревич	ru_RU
dc.contributor.author	Каюмов Айрат Рашитович	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/?p_id=153801	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	Статьи в зарубежных журналах и сборниках	ru_RU