Russian Journal of Biological Physics and Chemisrty Russian Journal of Biological Physics and Chemisrty АКТУАЛЬНЫЕ ВОПРОСЫ БИОЛОГИЧЕСКОЙ ФИЗИКИ И ХИМИИ 2499-9962 54580 МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ MEDICAL BIOPHYSICS AND BIOPHYSICAL CHEMISTRY МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ Landscape of mutation substitutions in yeast arginine CAN1 permease Распределение мутаций в молекуле белка дрожжевой аргинин пермиазы CAN1 Колтовая Н. А. Koltovaya N. A. koltovaya@jinr.ru Жучкина Н И Zhuchkina N I Душанов Э. Б. Dushanov E. B. Объединенный институт ядерных исследований Дубна Россия Joint Institute for Nuclear Research Dubna Russian Federation Объединенный институт ядерных исследований ru Joint Institute for Nuclear Research ru Объединенный институт ядерных исследований Дубна Россия Joint Institute for Nuclear Research Dubna Russian Federation 25 12 2020 25 12 2020 5 4 644 651 20 12 2020 20 12 2020 https://rusjbpc.ru/en/nauka/article/54580/view

При изучении закономерностей мутагенеза у дрожжей часто используют возникновение прямых мутаций в гене аргинин пермиазы CAN1 , нарушение которого приводит к канаванин-резистентности. Нами получена представительная коллекция мутаций can1 , позволяющая провести мутационный анализ структуры аргинин пермиазы. Этот фермент относится к суперсемейству транспортеров, переносящих аминокислоты через клеточные мембраны. Несмотря на несхожесть последовательностей, они обладают схожей структурой. Эукариотическая аргинин пермиаза может служить моделью для изучения структуры и функционирования аналогичных транспортеров. Изучение транспорта аргинина имеет особое значение в связи с тем, что аргинин является одним из ключевых метаболитов в процессах азотистого обмена. Аргинин является субстратом NO-синтаз в синтезе оксида азота NO, универсального трансмиттера, нейромедиатора и участника программируемой гибели клеток.

The occurrence of forward mutations in the arginine permease CAN1 gene, where damage leads to canavanine resistance, is often used to study mutagenesis in yeasts. We have obtained a representative collection of can1 mutations, which enables the mutational analysis of the arginine permease structure. This transport enzyme belongs to the APC superfamily supplying amino acids to cells. Despite sequence nonidentity, they have a similar structure. Eukaryotic arginine permease can serve as a model for the analysis of the structure and functioning of similar transporters. Studying arginine transport is of particular importance due to arginine being one of the key metabolites in nitrogen metabolism. Arginine is the NO-synthase substrate in NO synthesis, universal transmitter, neuromediator and actor of programmed cell death.

 аргинин пермиаза транспортеры АРС-суперсемейства мутационный анализ структуры фермента arginine permease conveyors ARS-supersmash mutational analysis of the structure of the enzyme

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