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Ribosomal RNA modification enzymes stimulate large ribosome subunit assembly in E. coli.
- Source :
-
Nucleic acids research [Nucleic Acids Res] 2024 Jun 24; Vol. 52 (11), pp. 6614-6628. - Publication Year :
- 2024
-
Abstract
- Ribosomal RNA modifications are introduced by specific enzymes during ribosome assembly in bacteria. Deletion of individual modification enzymes has a minor effect on bacterial growth, ribosome biogenesis, and translation, which has complicated the definition of the function of the enzymes and their products. We have constructed an Escherichia coli strain lacking 10 genes encoding enzymes that modify 23S rRNA around the peptidyl-transferase center. This strain exhibits severely compromised growth and ribosome assembly, especially at lower temperatures. Re-introduction of the individual modification enzymes allows for the definition of their functions. The results demonstrate that in addition to previously known RlmE, also RlmB, RlmKL, RlmN and RluC facilitate large ribosome subunit assembly. RlmB and RlmKL have functions in ribosome assembly independent of their modification activities. While the assembly stage specificity of rRNA modification enzymes is well established, this study demonstrates that there is a mutual interdependence between the rRNA modification process and large ribosome subunit assembly.<br /> (© The Author(s) 2024. Published by Oxford University Press on behalf of Nucleic Acids Research.)
- Subjects :
- Ribosome Subunits, Large, Bacterial metabolism
Ribosome Subunits, Large, Bacterial genetics
Methyltransferases metabolism
Methyltransferases genetics
RNA, Ribosomal metabolism
RNA, Ribosomal genetics
Ribosome Subunits, Large metabolism
Ribosome Subunits, Large genetics
Ribosomes metabolism
Ribosomes genetics
Escherichia coli genetics
Escherichia coli metabolism
Escherichia coli Proteins metabolism
Escherichia coli Proteins genetics
RNA, Ribosomal, 23S metabolism
RNA, Ribosomal, 23S genetics
RNA, Ribosomal, 23S chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1362-4962
- Volume :
- 52
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Nucleic acids research
- Publication Type :
- Academic Journal
- Accession number :
- 38554109
- Full Text :
- https://doi.org/10.1093/nar/gkae222