KFU. Card publication. Analysis of the mechanism of Mg2+ action on the RNase activity of Serratia marcescens endonuclease

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FEDERAL UNIVERSITY

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ANALYSIS OF THE MECHANISM OF MG2+ ACTION ON THE RNASE ACTIVITY OF SERRATIA MARCESCENS ENDONUCLEASE

Form of presentation

Articles in international journals and collections

Year of publication

2017

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Authors, employees of KFU

Zaynutdinova Elmira Faritovna, author

Romanova Yuliya Dzhafarovna, author

Filimonova Mariya Nikolaevna, author

Other authors

Gubskaya Valentina Petrovna, author

Bibliographic description in the original language

Romanova J. Analysis of the mechanism of Mg2+ action on the RNase activity of Serratia marcescens endonuclease // J.Romanova, V. Gubskaya, I.Nuretdinov, E. Zainutdinova, M. Filimonova//BioNanoScience. -2017.-V.2.- P.276-283

Annotation

The main goal of the investigation was to analyzeto analyze the mechanism of Mg2+ action on the digestive activity of Serratia marcescens nuclease towards RNA due to the potential application of the nuclease as a reagent for removing nucleic acids from biomedical samples as well as an antiviral factor. Examination of the mechanism revealed that it was similar to the mechanism of the metals actions on the DNase activity. The optimal Mg2+ amount was linked with the changing secondary structure of RNA - substrates within A-helix. Addition of Mg2+ was found to affect both the rates of products dissociations from the enzyme-substrate complexes and the enzyme associations with the substrates, that was supported by strong increase in the Kcat values and change in the Km values . values. Comparing the mechanisms of Mg2+ action on RNase and DNase activities in S. marcescens nuclease, we identified a preference for DNA in the absence of Mg2+ shown that was supported by with the higher Kcat values

Keywords

Serratia marcescens nuclease, the mechanism of Mg2+ action on the RNase activity ,activity, preference for DNA substrate

The name of the journal

BioNanoScience

URL

http://link.springer.com/article/10.1007/s12668-016-0358-y

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

https://repository.kpfu.ru/eng/?p_id=146403&p_lang=2

Resource files

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art%3A10.1007%2Fs12668_016_0358_y.pdf	1,32	pdf	show / download

Full metadata record

Field DC	Value	Language
dc.contributor.author	Zaynutdinova Elmira Faritovna	ru_RU
dc.contributor.author	Romanova Yuliya Dzhafarovna	ru_RU
dc.contributor.author	Filimonova Mariya Nikolaevna	ru_RU
dc.contributor.author	Gubskaya Valentina Petrovna	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	Romanova J. Analysis of the mechanism of Mg2+ action on the RNase activity of Serratia marcescens endonuclease // J.Romanova, V. Gubskaya, I.Nuretdinov, E. Zainutdinova, M. Filimonova//BioNanoScience. -2017.-V.2.- P.276-283	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=146403&p_lang=2	ru_RU
dc.description.abstract	BioNanoScience	ru_RU
dc.description.abstract	The main goal of the investigation was to analyzeto analyze the mechanism of Mg2+ action on the digestive activity of Serratia marcescens nuclease towards RNA due to the potential application of the nuclease as a reagent for removing nucleic acids from biomedical samples as well as an antiviral factor. Examination of the mechanism revealed that it was similar to the mechanism of the metals actions on the DNase activity. The optimal Mg2+ amount was linked with the changing secondary structure of RNA - substrates within A-helix. Addition of Mg2+ was found to affect both the rates of products dissociations from the enzyme-substrate complexes and the enzyme associations with the substrates, that was supported by strong increase in the Kcat values and change in the Km values . values. Comparing the mechanisms of Mg2+ action on RNase and DNase activities in S. marcescens nuclease, we identified a preference for DNA in the absence of Mg2+ shown that was supported by with the higher Kcat values	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	Serratia marcescens nuclease	ru_RU
dc.subject	the mechanism of Mg2+ action on the RNase activity	ru_RU
dc.subject	activity	ru_RU
dc.subject	preference for DNA substrate	ru_RU
dc.title	Analysis of the mechanism of Mg2+ action on the RNase activity of Serratia marcescens endonuclease	ru_RU
dc.type	Articles in international journals and collections	ru_RU