Cargando…
Structure and mechanistic features of the prokaryotic minimal RNase P
Endonucleolytic removal of 5’-leader sequences from tRNA precursor transcripts (pre-tRNAs) by ribonuclease P (RNase P) is essential for protein synthesis. Beyond RNA-based RNase P enzymes, protein-only versions of the enzyme exert this function in various eukarya (there termed PRORPs) and in some ba...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8266387/ https://www.ncbi.nlm.nih.gov/pubmed/34180399 http://dx.doi.org/10.7554/eLife.70160 |
_version_ | 1783719936408944640 |
---|---|
author | Feyh, Rebecca Waeber, Nadine B Prinz, Simone Giammarinaro, Pietro Ivan Bange, Gert Hochberg, Georg Hartmann, Roland K Altegoer, Florian |
author_facet | Feyh, Rebecca Waeber, Nadine B Prinz, Simone Giammarinaro, Pietro Ivan Bange, Gert Hochberg, Georg Hartmann, Roland K Altegoer, Florian |
author_sort | Feyh, Rebecca |
collection | PubMed |
description | Endonucleolytic removal of 5’-leader sequences from tRNA precursor transcripts (pre-tRNAs) by ribonuclease P (RNase P) is essential for protein synthesis. Beyond RNA-based RNase P enzymes, protein-only versions of the enzyme exert this function in various eukarya (there termed PRORPs) and in some bacteria (Aquifex aeolicus and close relatives); both enzyme types belong to distinct subgroups of the PIN domain metallonuclease superfamily. Homologs of Aquifex RNase P (HARPs) are also expressed in some other bacteria and many archaea, where they coexist with RNA-based RNase P and do not represent the main RNase P activity. Here, we solved the structure of the bacterial HARP from Halorhodospira halophila by cryo-electron microscopy, revealing a novel screw-like dodecameric assembly. Biochemical experiments demonstrate that oligomerization is required for RNase P activity of HARPs. We propose that the tRNA substrate binds to an extended spike-helix (SH) domain that protrudes from the screw-like assembly to position the 5’-end in close proximity to the active site of the neighboring dimer. The structure suggests that eukaryotic PRORPs and prokaryotic HARPs recognize the same structural elements of pre-tRNAs (tRNA elbow region and cleavage site). Our analysis thus delivers the structural and mechanistic basis for pre-tRNA processing by the prokaryotic HARP system. |
format | Online Article Text |
id | pubmed-8266387 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-82663872021-07-12 Structure and mechanistic features of the prokaryotic minimal RNase P Feyh, Rebecca Waeber, Nadine B Prinz, Simone Giammarinaro, Pietro Ivan Bange, Gert Hochberg, Georg Hartmann, Roland K Altegoer, Florian eLife Biochemistry and Chemical Biology Endonucleolytic removal of 5’-leader sequences from tRNA precursor transcripts (pre-tRNAs) by ribonuclease P (RNase P) is essential for protein synthesis. Beyond RNA-based RNase P enzymes, protein-only versions of the enzyme exert this function in various eukarya (there termed PRORPs) and in some bacteria (Aquifex aeolicus and close relatives); both enzyme types belong to distinct subgroups of the PIN domain metallonuclease superfamily. Homologs of Aquifex RNase P (HARPs) are also expressed in some other bacteria and many archaea, where they coexist with RNA-based RNase P and do not represent the main RNase P activity. Here, we solved the structure of the bacterial HARP from Halorhodospira halophila by cryo-electron microscopy, revealing a novel screw-like dodecameric assembly. Biochemical experiments demonstrate that oligomerization is required for RNase P activity of HARPs. We propose that the tRNA substrate binds to an extended spike-helix (SH) domain that protrudes from the screw-like assembly to position the 5’-end in close proximity to the active site of the neighboring dimer. The structure suggests that eukaryotic PRORPs and prokaryotic HARPs recognize the same structural elements of pre-tRNAs (tRNA elbow region and cleavage site). Our analysis thus delivers the structural and mechanistic basis for pre-tRNA processing by the prokaryotic HARP system. eLife Sciences Publications, Ltd 2021-06-28 /pmc/articles/PMC8266387/ /pubmed/34180399 http://dx.doi.org/10.7554/eLife.70160 Text en © 2021, Feyh et al https://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Biochemistry and Chemical Biology Feyh, Rebecca Waeber, Nadine B Prinz, Simone Giammarinaro, Pietro Ivan Bange, Gert Hochberg, Georg Hartmann, Roland K Altegoer, Florian Structure and mechanistic features of the prokaryotic minimal RNase P |
title | Structure and mechanistic features of the prokaryotic minimal RNase P |
title_full | Structure and mechanistic features of the prokaryotic minimal RNase P |
title_fullStr | Structure and mechanistic features of the prokaryotic minimal RNase P |
title_full_unstemmed | Structure and mechanistic features of the prokaryotic minimal RNase P |
title_short | Structure and mechanistic features of the prokaryotic minimal RNase P |
title_sort | structure and mechanistic features of the prokaryotic minimal rnase p |
topic | Biochemistry and Chemical Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8266387/ https://www.ncbi.nlm.nih.gov/pubmed/34180399 http://dx.doi.org/10.7554/eLife.70160 |
work_keys_str_mv | AT feyhrebecca structureandmechanisticfeaturesoftheprokaryoticminimalrnasep AT waebernadineb structureandmechanisticfeaturesoftheprokaryoticminimalrnasep AT prinzsimone structureandmechanisticfeaturesoftheprokaryoticminimalrnasep AT giammarinaropietroivan structureandmechanisticfeaturesoftheprokaryoticminimalrnasep AT bangegert structureandmechanisticfeaturesoftheprokaryoticminimalrnasep AT hochberggeorg structureandmechanisticfeaturesoftheprokaryoticminimalrnasep AT hartmannrolandk structureandmechanisticfeaturesoftheprokaryoticminimalrnasep AT altegoerflorian structureandmechanisticfeaturesoftheprokaryoticminimalrnasep |