КФУ. Карточка публикации. Structure and molecular characterization of diadenosine polyphosphate hydrolase in Brachypodium distachyon

КАЗАНСКИЙ
ФЕДЕРАЛЬНЫЙ УНИВЕРСИТЕТ

RUS

- EN
- 中文
- ES

STRUCTURE AND MOLECULAR CHARACTERIZATION OF DIADENOSINE POLYPHOSPHATE HYDROLASE IN BRACHYPODIUM DISTACHYON

Форма представления

Статьи в зарубежных журналах и сборниках

Год публикации

2018

Язык

английский

Авторы, сотрудники КФУ

Сабиров Рушан Мирзович, автор

Ямщиков Игорь Вячеславович, автор

Другие авторы

Sugimoto Manabu , автор

Библиографическое описание на языке оригинала

Tanaka M., Iamshchikov I., KatoY., Sabirov R., Gusev O., Sakamoto W. and Sugimoto M. Structure and molecular characterization of diadenosine polyphosphate hydrolase in Brachypodium distachyon // J Plant Biochem Physiol, an open access journal, 2018. – V. 6, Is. 3. – 7 p. DOI: 10.4172/2329-9029.1000220

Аннотация

Putative diadenosine polyphosphate (ApnA) hydrolase gene, which encodes an amino acid sequence showing homology with that of Arabidopsis long-chain (ApnA) (n=5–6) hydrolase (AtNUDX13) and which conserves nudix motif and glycine tripeptide motif, was identified from Brachypodium distachyon. The mature form of Brachypodium (ApnA) hydrolase (BraNUDX15) catalyzed long-chain (ApnA) and Ap4A, Ap4G, Gp4G, and dCTP, showing different substrate specificity from Arabidopsis (ApnA) hydrolases AtNUDX13, 25, 26, and 27. BraNUDX15 required Mg2+ and produced ATP from (ApnA), indicating asymmetrical (ApnA) hydrolase as the same as Arabidopsis (ApnA) hydrolases. Results show that BraNUDX15 gene was up-regulated by UV-A, UV-B, and UV-C irradiation and downregulated by drought stress, but it was left unchanged by salt stress. Subcellular localization indicated that the BraNUDX15 protein was colocalized with the surface of the chloroplasts.

Ключевые слова

Brachypodium distachyon, diadenosine polyphosphate, drought stress, nudix hydrolase, UV irradiation

Название журнала

Journal of Plant Biochemistry & Physiology

URL

https://www.omicsonline.org/open-access/structure-and-molecular-characterization-of-diadenosine-polyphosphatehydrolase-in-brachypodium-distachyon-2329-9029-1000220.pdf

Пожалуйста, используйте этот идентификатор, чтобы цитировать или ссылаться на эту карточку

https://repository.kpfu.ru/?p_id=188798

Файлы ресурса

Название файла	Размер (Мб)	Формат
F_Tanaka_Iamshikov_Sabirov_et_all_J_Plant_Biochem_Physiol_2018.pdf	0,51	pdf	посмотреть / скачать

Полная запись метаданных

Поле DC	Значение	Язык
dc.contributor.author	Сабиров Рушан Мирзович	ru_RU
dc.contributor.author	Ямщиков Игорь Вячеславович	ru_RU
dc.contributor.author	Sugimoto Manabu	ru_RU
dc.date.accessioned	2018-01-01T00:00:00Z	ru_RU
dc.date.available	2018-01-01T00:00:00Z	ru_RU
dc.date.issued	2018	ru_RU
dc.identifier.citation	Tanaka M., Iamshchikov I., KatoY., Sabirov R., Gusev O., Sakamoto W. and Sugimoto M. Structure and molecular characterization of diadenosine polyphosphate hydrolase in Brachypodium distachyon // J Plant Biochem Physiol, an open access journal, 2018. – V. 6, Is. 3. – 7 p. DOI: 10.4172/2329-9029.1000220	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/?p_id=188798	ru_RU
dc.description.abstract	Journal of Plant Biochemistry & Physiology	ru_RU
dc.description.abstract	Putative diadenosine polyphosphate (ApnA) hydrolase gene, which encodes an amino acid sequence showing homology with that of Arabidopsis long-chain (ApnA) (n=5–6) hydrolase (AtNUDX13) and which conserves nudix motif and glycine tripeptide motif, was identified from Brachypodium distachyon. The mature form of Brachypodium (ApnA) hydrolase (BraNUDX15) catalyzed long-chain (ApnA) and Ap4A, Ap4G, Gp4G, and dCTP, showing different substrate specificity from Arabidopsis (ApnA) hydrolases AtNUDX13, 25, 26, and 27. BraNUDX15 required Mg2+ and produced ATP from (ApnA), indicating asymmetrical (ApnA) hydrolase as the same as Arabidopsis (ApnA) hydrolases. Results show that BraNUDX15 gene was up-regulated by UV-A, UV-B, and UV-C irradiation and downregulated by drought stress, but it was left unchanged by salt stress. Subcellular localization indicated that the BraNUDX15 protein was colocalized with the surface of the chloroplasts.	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	Brachypodium distachyon	ru_RU
dc.subject	diadenosine polyphosphate	ru_RU
dc.subject	drought stress	ru_RU
dc.subject	nudix hydrolase	ru_RU
dc.subject	UV irradiation	ru_RU
dc.title	Structure and molecular characterization of diadenosine polyphosphate hydrolase in Brachypodium distachyon	ru_RU
dc.type	Статьи в зарубежных журналах и сборниках	ru_RU