KFU. Card publication. The Temperature-Dependent Selectivity of Potential Interaction Partners for the Small Heat Shock Protein IbpA from Acholeplasma laidlawii

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THE TEMPERATURE-DEPENDENT SELECTIVITY OF POTENTIAL INTERACTION PARTNERS FOR THE SMALL HEAT SHOCK PROTEIN IBPA FROM ACHOLEPLASMA LAIDLAWII

Form of presentation

Articles in international journals and collections

Year of publication

2016

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Authors, employees of KFU

Kayumov Ayrat Rashitovich, author

Other authors

Bogachev Mikhail Igorevich, author

Borshheus Sergey , author

Vishnyakov Innokentiy , author

Authors, postgraduates KFU

Salafutdinov Ilnur Ildusovich, postgraduate kfu

Bibliographic description in the original language

Vishnyakov I.E. The Temperature-Dependent Selectivity of Potential Interaction Partners for the Small Heat Shock Protein IbpA from Acholeplasma laidlawii /I.E. Vishnyakov, M. Bogachev, I. Salafutdinov, S.N. Borchsenius, A.R. Kayumov // BioNanoScience. - 2016. DOI: 10.1007/s12668-016-0259-0.

Annotation

Small heat shock proteins (sHsps) of α-crystalline type play a key role in the cell survival under stress conditions by preventing irreversible denaturation and aggregation of proteins. In contrast to most Mollicutes (mycoplasmas) where no sHsps were found, recently, some sHsp homologs were identified in the Acholeplasmataceae family, including Acholeplasma laidlawii, the only representative of Mollicutes that is known to survive in a host-free environment. Using pull-down followed by LC-MS, we identified the potential target proteins co-eluting with IbpA from the A. laidlawii cell extracts after exposition to low- and high temperatures. 308 and 464 proteins were co-eluted with IbpA from the cold- and heat-treated extracts, respectively, while only 240 of them were co-eluted with sHsp independently of the temperature. Most of potential IbpA targets were identified as enzymes involved in biosynthetic cycles and energy metabolism. We show IbpA specificity for target proteins on the incub

Keywords

Acholeplasma laidlawii, Small heat shockproteins (sHsps), IbpA, Heat shock, Cold shock

The name of the journal

BioNanoScience

URL

https://www.researchgate.net/publication/307561121_The_Temperature-Dependent_Selectivity_of_Potential_Interaction_Partners_for_the_Small_Heat_Shock_Protein_IbpA_from_Acholeplasma_laidlawii

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

https://repository.kpfu.ru/eng/?p_id=138233&p_lang=2

Full metadata record

Field DC	Value	Language
dc.contributor.author	Kayumov Ayrat Rashitovich	ru_RU
dc.contributor.author	Bogachev Mikhail Igorevich	ru_RU
dc.contributor.author	Borshheus Sergey	ru_RU
dc.contributor.author	Vishnyakov Innokentiy	ru_RU
dc.contributor.author	Salafutdinov Ilnur Ildusovich	ru_RU
dc.date.accessioned	2016-01-01T00:00:00Z	ru_RU
dc.date.available	2016-01-01T00:00:00Z	ru_RU
dc.date.issued	2016	ru_RU
dc.identifier.citation	Vishnyakov I.E. The Temperature-Dependent Selectivity of Potential Interaction Partners for the Small Heat Shock Protein IbpA from Acholeplasma laidlawii /I.E. Vishnyakov, M. Bogachev, I. Salafutdinov, S.N. Borchsenius, A.R. Kayumov // BioNanoScience. - 2016. DOI: 10.1007/s12668-016-0259-0.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=138233&p_lang=2	ru_RU
dc.description.abstract	BioNanoScience	ru_RU
dc.description.abstract	Small heat shock proteins (sHsps) of α-crystalline type play a key role in the cell survival under stress conditions by preventing irreversible denaturation and aggregation of proteins. In contrast to most Mollicutes (mycoplasmas) where no sHsps were found, recently, some sHsp homologs were identified in the Acholeplasmataceae family, including Acholeplasma laidlawii, the only representative of Mollicutes that is known to survive in a host-free environment. Using pull-down followed by LC-MS, we identified the potential target proteins co-eluting with IbpA from the A. laidlawii cell extracts after exposition to low- and high temperatures. 308 and 464 proteins were co-eluted with IbpA from the cold- and heat-treated extracts, respectively, while only 240 of them were co-eluted with sHsp independently of the temperature. Most of potential IbpA targets were identified as enzymes involved in biosynthetic cycles and energy metabolism. We show IbpA specificity for target proteins on the incub	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	Acholeplasma laidlawii	ru_RU
dc.subject	Small heat shockproteins (sHsps)	ru_RU
dc.subject	IbpA	ru_RU
dc.subject	Heat shock	ru_RU
dc.subject	Cold shock	ru_RU
dc.title	The Temperature-Dependent Selectivity of Potential Interaction Partners for the Small Heat Shock Protein IbpA from Acholeplasma laidlawii	ru_RU
dc.type	Articles in international journals and collections	ru_RU