Structural and Functional Differences between Homologous Bacterial Ribonucleases

Structural and Functional Differences between Homologous Bacterial Ribonucleases Научная публикация

Журнал

International Journal of Molecular Sciences
, E-ISSN: 1422-0067

Вых. Данные

Год: 2022, Том: 23, Номер: 3, Номер статьи : 1867, Страниц : DOI: 10.3390/ijms23031867

Ключевые слова

ribonuclease; binase; balnase; barnase; balifase; ribonuclease inhibitor; barstar; catalytic activity; structural organization

Авторы

Ulyanova Vera ¹ , Nadyrova Alsu ¹ , Dudkina Elena ¹ , Kuznetsova Aleksandra ² , Ahmetgalieva Albina ¹ , Faizullin Dzhigangir ³ , Surchenko Yulia ¹ , Novopashina Darya ² , Zuev Yuriy ³ , Kuznetsov Nikita ² , Ilinskaya Olga ¹

Организации

1	(Данные Web of science) Kazan Volga Reg Fed Univ, Inst Fundamental Med & Biol, Dept Microbiol, Kazan 420008, Russia
2	(Данные Web of science) Russian Acad Sci, Inst Chem Biol & Fundamental Med, Siberian Branch, Novosibirsk 630090, Russia
3	(Данные Web of science) FRC Kazan Sci Ctr RAS, Kazan Inst Biochem & Biophys, Kazan 420111, Russia

Small cationic guanyl-preferring ribonucleases (RNases) produced by the Bacillus species share a similar protein tertiary structure with a high degree of amino acid sequence conservation. However, they form dimers that differ in conformation and stability. Here, we have addressed the issues (1) whether the homologous RNases also have distinctions in catalytic activity towards different RNA substrates and interactions with the inhibitor protein barstar, and (2) whether these differences correlate with structural features of the proteins. Circular dichroism and dynamic light scattering assays revealed distinctions in the structures of homologous RNases. The activity levels of the RNases towards natural RNA substrates, as measured spectrometrically by acid-soluble hydrolysis products, were similar and decreased in the row high-polymeric RNA >>> transport RNA > double-stranded RNA. However, stopped flow kinetic studies on model RNA substrates containing the guanosine residue in a hairpin stem or a loop showed that the cleavage rates of these enzymes were different. Moreover, homologous RNases were inhibited by the barstar with diverse efficiency. Therefore, minor changes in structure elements of homologous proteins have a potential to significantly effect molecule stability and functional activities, such as catalysis or ligand binding.

Ulyanova V. , Nadyrova A. , Dudkina E. , Kuznetsova A. , Ahmetgalieva A. , Faizullin D. , Surchenko Y. , Novopashina D. , Zuev Y. , Kuznetsov N. , Ilinskaya O.
Structural and Functional Differences between Homologous Bacterial Ribonucleases
International Journal of Molecular Sciences. 2022. V.23. N3. 1867 . DOI: 10.3390/ijms23031867 WOS Scopus OpenAlex

Опубликована в печати:

7 февр. 2022 г.

Web of science:	WOS:000756428900001
Scopus:	2-s2.0-85124091370
OpenAlex:	W4210942291

БД	Цитирований
Web of science	3
Scopus	3
OpenAlex	4