KFU. Card publication. New insight into secreted ribonuclease structure: binase is a natural dimer

KAZAN
FEDERAL UNIVERSITY

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- 中文
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NEW INSIGHT INTO SECRETED RIBONUCLEASE STRUCTURE: BINASE IS A NATURAL DIMER

Form of presentation

Articles in international journals and collections

Year of publication

2014

Язык

английский

Authors, employees of KFU

Dudkina Elena Vladimirovna, author

Ilinskaya Olga Nikolaevna, author

Kayumov Ayrat Rashitovich, author

Bibliographic description in the original language

Dudkina E. New insight into secreted ribonuclease structure: binase is a natural dimer / Dudkina E., Kayumov A., Ulyanova V., Ilinskaya O. // PLoS One. - 2014. - V. 9(12). - P. e115818. doi:10.1371/journal.pone.0115818.

Annotation

The biological effects of ribonucleases (RNases), such as the control of the blood vessels growth, the toxicity towards tumour cells and antiviral activity, require a detailed explanation. One of the most intriguing properties of RNases which can contribute to their biological effects is the ability to form dimers, which facilitates efficient RNA hydrolysis and the evasion of ribonuclease inhibitor. Dimeric forms of microbial RNase binase secreted by Bacillus pumilus (former B. intermedius) have only been found in crystals to date. Our study is the first report directly confirming the existence of binase dimers in solution and under natural conditions of enzyme biosynthesis and secretion by bacilli. Using different variants of gel electrophoresis, immunoblotting, size-exclusion chromatography and mass-spectrometry, we revealed that binase is a stable natural dimer with high catalytic activity.

Keywords

ribonuclease, binase, dimer

The name of the journal

PLos ONE

URL

http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0115818

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

https://repository.kpfu.ru/eng/?p_id=88343&p_lang=2

Resource files

File name	Size (MB)	Format
journal.pone.0115818.pdf	0,87	pdf	show / download

Full metadata record

Field DC	Value	Language
dc.contributor.author	Dudkina Elena Vladimirovna	ru_RU
dc.contributor.author	Ilinskaya Olga Nikolaevna	ru_RU
dc.contributor.author	Kayumov Ayrat Rashitovich	ru_RU
dc.date.accessioned	2014-01-01T00:00:00Z	ru_RU
dc.date.available	2014-01-01T00:00:00Z	ru_RU
dc.date.issued	2014	ru_RU
dc.identifier.citation	Dudkina E. New insight into secreted ribonuclease structure: binase is a natural dimer / Dudkina E., Kayumov A., Ulyanova V., Ilinskaya O. // PLoS One. - 2014. - V. 9(12). - P. e115818. doi:10.1371/journal.pone.0115818.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=88343&p_lang=2	ru_RU
dc.description.abstract	PLos ONE	ru_RU
dc.description.abstract	The biological effects of ribonucleases (RNases), such as the control of the blood vessels growth, the toxicity towards tumour cells and antiviral activity, require a detailed explanation. One of the most intriguing properties of RNases which can contribute to their biological effects is the ability to form dimers, which facilitates efficient RNA hydrolysis and the evasion of ribonuclease inhibitor. Dimeric forms of microbial RNase binase secreted by Bacillus pumilus (former B. intermedius) have only been found in crystals to date. Our study is the first report directly confirming the existence of binase dimers in solution and under natural conditions of enzyme biosynthesis and secretion by bacilli. Using different variants of gel electrophoresis, immunoblotting, size-exclusion chromatography and mass-spectrometry, we revealed that binase is a stable natural dimer with high catalytic activity.	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	ribonuclease	ru_RU
dc.subject	binase	ru_RU
dc.subject	dimer	ru_RU
dc.title	New insight into secreted ribonuclease structure: binase is a natural dimer	ru_RU
dc.type	Articles in international journals and collections	ru_RU