Russian Journal of Biological Physics and Chemisrty Russian Journal of Biological Physics and Chemisrty АКТУАЛЬНЫЕ ВОПРОСЫ БИОЛОГИЧЕСКОЙ ФИЗИКИ И ХИМИИ 2499-9962 54190 МОЛЕКУЛЯРНАЯ БИОФИЗИКА И ФИЗИКА БИОМОЛЕКУЛ MOLECULAR BIOPHYSICS AND PHYSICS OF BIOMOLECULES МОЛЕКУЛЯРНАЯ БИОФИЗИКА И ФИЗИКА БИОМОЛЕКУЛ The role of contacts of N-terminal region of protein l27 with ribosomal 23s RNA in the formation of the functionally active bacterial ribosomes Роль контактов n-концевого участка белка L27 с рибосомной 23S РНК в формировании функционально-активной бактериальной рибосомы Фандо М С Fando M S fando@vega.protres.ru Коробейникова А В Korobeinikova A V Институт белка РАН ru Institute of Protein Research RAS ru Институт белка РАН ru Institute of Protein Research RAS ru 25 06 2017 25 06 2017 2 1 351 355 20 06 2017 20 06 2017 https://rusjbpc.ru/en/nauka/article/54190/view

Рибосомный белок L27 является особенностью бактериальной рибосомы. Из результатов структурных исследований известно, что вытянутый N-концевой «хвост» белка L27 достигает пептидилтрансферазного центра рибосомы, где он образует обширные контакты cо спиралями Н80-Н81 23S рРНК, а также несколько контактов с тРНК в А- и Р-участках рибосомы. Укорочение белка L27 из Escherichia coli с N-конца приводит к снижению функциональной активности рибосом. Предполагается, что белок L27 играет важную роль в позиционировании тРНК в двух тРНК-связывающих сайтах рибосомы. В настоящей работе исследована роль контактов N-концевого участка белка L27 с 23S рРНК в функционировании рибосомы. С этой целью был создан ряд штаммов E. coli , содержащих белок L27 с точечными заменами. Оказалось, что некоторые внесенные в белок замены (K4L или K4A/K5G) приводят к значительному замедлению роста клеток и снижению активности их аппарата трансляции. На основании имеющихся структурных данных в рибосоме эти консервативные аминокислотные остатки белка L27 взаимодействуют только с 23S рРНК, но не с тРНК. Полученные в работе данные указывают на важность контактов N-концевого участка белка L27 с 23S рРНК для формирования функционально-активной бактериальной рибосомы in vivo .

Ribosomal protein L27 is a feature of the bacterial ribosome. Based on structural studies, the extended N- terminal tail of protein L27 is known to reach the peptidyl transferase center of the ribosome, where it forms the extensive contacts with helixes H80-H81 of the 23S rRNA as well as several contacts with tRNAs at the A- and P-sites. Shortening of the Escherichia coli protein L27 from N-terminus led to the decrease of the functional activity of the ribosomes. It is supposed that protein L27 plays an important role in the positioning of tRNA in two tRNA-binding sites of the ribosome. In the present work, the role of the contacts of the N-terminal region of protein L27 with the 23S rRNA in the function of the ribosome has been investigated. For this purpose, a number of E. coli strains have been constructed containing protein L27 with the point replacements. It has turned out that some replacements (K4L or K4A/K5G) introduced into the protein lead to the significant slowdown of the cell growth and the decrease in the activity of their translation apparatus. Based on the available structural data, within the ribosome these conservative amino acid residues of protein L27 form the contacts only with 23S rRNA but not with tRNA. The data obtained in the work indicate the importance of the contacts of N-terminal region of protein L27 with the 23S rRNA for the formation of the functionally active bacterial ribosome in vivo .

 рибосомный белок L27 рибосомная РНК рибосома трансляция Escherichia coli ribosomal protein L27 ribosomal RNA ribosome translation Escherichia coli

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