Ribosomal protein uS7/Rps5 serine-223 in protein kinase-mediated phosphorylation and ribosomal small subunit maturation

Makoto Tomioka, Mitsugu Shimobayashi, Makoto Kitabatake, Mutsuhito Ohno, Yasunori Kozutsumi, Shogo Oka, Hiromu Takematsu

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Cellular translation should be precisely controlled in response to extracellular cues. However, knowledge is limited concerning signal transduction-regulated translation. In the present study, phosphorylation was identified in the 40S small subunit ribosomal protein uS7 (Yjr123w/previously called as Rps5) by Ypk1 and Pkc1, AGC family protein kinases in yeast Saccharomyces cerevisiae. Serine residue 223 (Ser223) of uS7 in the conserved C-terminal region was crucial for this phosphorylation event. S223A mutant uS7 caused severe reduction of small ribosomal subunit production, likely due to compromised interaction with Rio2, resulting in both reduced translation and reduced cellular proliferation. Contrary to optimal culture conditions, heat stressed S223A mutant cells exhibited increased heat resistance and induced heat shock proteins. Taken together, an intracellular signal transduction pathway involving Ypk1/Pkc1 seemed to play an important role in ribosome biogenesis and subsequent cellular translation, utilizing uS7 as a substrate.

Original languageEnglish
Article number1244
JournalScientific reports
Volume8
Issue number1
DOIs
Publication statusPublished - 01-12-2018

All Science Journal Classification (ASJC) codes

  • General

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