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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...

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Autores principales: Feyh, Rebecca, Waeber, Nadine B, Prinz, Simone, Giammarinaro, Pietro Ivan, Bange, Gert, Hochberg, Georg, Hartmann, Roland K, Altegoer, Florian
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
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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.
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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
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