Isolation and characterization of a dominant negative mutant of Bacillus subtilis GTP-binding protein, YlqF, essential for biogenesis and maintenance of the 50 S ribosomal subunit

Yoshitaka Matsuo, Taku Oshima, Chin Loh Pek, Takuya Morimoto, Naotake Ogasawara

研究成果: Article査読

21 被引用数 (Scopus)

抄録

The circularly permuted GTPase YlqF is essential for cell viability and is broadly conserved from Gram-positive bacteria to eukaryotes. We previously reported that YlqF participates in the late step of 50 S ribosomal subunit assembly in Bacillus subtilis. Here, we demonstrate that an N-terminal deletion mutant of YlqF (YlqFΔN10) inhibits cell growth even in the presence of wild-type YlqF. In contrast to the wild-type protein, the GTPase activity of this mutant was not stimulated by the 50 S subunit and did not dissociate from the premature 50 S subunit. Thus, YlqFΔN10 acts as a competitive inhibitor of wild-type YlqF. Premature 50 S subunit lacking ribosomal protein L27 and with a reduced amount of L16 accumulated in YlqFΔN10-overexpressing cells and in YlqF-depleted cells, suggesting that YlqFΔN10 binds to the premature 50 S subunit. Moreover, premature 50 S subunit from both YlqFΔN10-overexpressing and YlqF-depleted cells more strongly enhanced the GTPase activity of YlqF than the mature 50 S subunit of the 70 S ribosome. Collectively, our results indicate that YlqF is targeted to the premature 50 S subunit lacking ribosomal proteins L16 and L27 to assemble functional 50 S subunit through a GTPase activity-dependent conformational change of 23 S rRNA.

本文言語English
ページ(範囲)25270-25277
ページ数8
ジャーナルJournal of Biological Chemistry
282
35
DOI
出版ステータスPublished - 2007 8 31

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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