Novel Essential Gene Involved in 16S rRNA Processing in Escherichia coli. Issue 4 (27th February 2015)
- Record Type:
- Journal Article
- Title:
- Novel Essential Gene Involved in 16S rRNA Processing in Escherichia coli. Issue 4 (27th February 2015)
- Main Title:
- Novel Essential Gene Involved in 16S rRNA Processing in Escherichia coli
- Authors:
- Kurata, Tatsuaki
Nakanishi, Shinobu
Hashimoto, Masayuki
Taoka, Masato
Yamazaki, Yukiko
Isobe, Toshiaki
Kato, Jun-ichi - Abstract:
- Abstract: Biogenesis of ribosomes is a complex process mediated by many factors. While its transcription proceeds, ribosomal RNA (rRNA) folds itself into a characteristic three-dimensional structure through interaction with ribosomal proteins, during which its ends are processed. Here, we show that the essential protein YqgF, a RuvC family protein with an RNase-H-like motif, is involved in the processing of pre-16S rRNA during ribosome maturation. Indeed, pre-16S rRNA accumulated in cells of a temperature-sensitive yqgF mutant ( yqgF ts ) cultured at a non-permissive temperature. In addition, purified YqgF was shown to process the 5′ end of pre-16S rRNA within 70S ribosomes in vitro . Mass spectrometry analysis of the total proteins in the yqgF ts mutant cells showed that the expression of genes containing multiple Shine–Dalgarno-like sequences was observed to be lower than in wild type. These results are interpreted to indicate that YqgF is involved in a novel enzymic activity necessary for the processing of pre-16S rRNA, thereby affecting elongation of translation. Graphical abstract: Highlights: Escherichia coli essential protein YqgF, a RuvC family protein with an RNase-H-like motif. Accumulation of pre-16S rRNA in cells of a temperature-sensitive yqgF mutant. In vitro processing of 5′ end of pre-16S rRNA within 70S ribosomes by purified YqgF. Lowered expression of genes containing multiple Shine–Dalgarno-like sequences. YqgF involved in ribosome maturation andAbstract: Biogenesis of ribosomes is a complex process mediated by many factors. While its transcription proceeds, ribosomal RNA (rRNA) folds itself into a characteristic three-dimensional structure through interaction with ribosomal proteins, during which its ends are processed. Here, we show that the essential protein YqgF, a RuvC family protein with an RNase-H-like motif, is involved in the processing of pre-16S rRNA during ribosome maturation. Indeed, pre-16S rRNA accumulated in cells of a temperature-sensitive yqgF mutant ( yqgF ts ) cultured at a non-permissive temperature. In addition, purified YqgF was shown to process the 5′ end of pre-16S rRNA within 70S ribosomes in vitro . Mass spectrometry analysis of the total proteins in the yqgF ts mutant cells showed that the expression of genes containing multiple Shine–Dalgarno-like sequences was observed to be lower than in wild type. These results are interpreted to indicate that YqgF is involved in a novel enzymic activity necessary for the processing of pre-16S rRNA, thereby affecting elongation of translation. Graphical abstract: Highlights: Escherichia coli essential protein YqgF, a RuvC family protein with an RNase-H-like motif. Accumulation of pre-16S rRNA in cells of a temperature-sensitive yqgF mutant. In vitro processing of 5′ end of pre-16S rRNA within 70S ribosomes by purified YqgF. Lowered expression of genes containing multiple Shine–Dalgarno-like sequences. YqgF involved in ribosome maturation and elongation of translation. … (more)
- Is Part Of:
- Journal of molecular biology. Volume 427:Issue 4(2015:Feb. 15)
- Journal:
- Journal of molecular biology
- Issue:
- Volume 427:Issue 4(2015:Feb. 15)
- Issue Display:
- Volume 427, Issue 4 (2015)
- Year:
- 2015
- Volume:
- 427
- Issue:
- 4
- Issue Sort Value:
- 2015-0427-0004-0000
- Page Start:
- 955
- Page End:
- 965
- Publication Date:
- 2015-02-27
- Subjects:
- rRNA ribosomal RNA -- SD Shine–Dalgarno -- WT wild type -- LC liquid chromatography -- MS mass spectrometry -- HJR Holliday junction resolvase
16S rRNA -- E. coli -- essential gene -- rRNA processing -- YqgF
Molecular biology -- Periodicals
Biology -- Periodicals
Biochemistry -- Periodicals
Bacteriology -- Periodicals
Molecular Biology -- Periodicals
Biochemistry -- Periodicals
Biologie moléculaire -- Périodiques
Biologie -- Périodiques
Biochimie -- Périodiques
Moleculaire biologie
Biochemistry
Biology
Molecular biology
Periodicals
572.805 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00222836 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.jmb.2014.12.013 ↗
- Languages:
- English
- ISSNs:
- 0022-2836
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5020.700000
British Library DSC - BLDSS-3PM
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- 10729.xml