Skip to main content
bioRxiv
  • Home
  • About
  • Submit
  • ALERTS / RSS
Advanced Search
New Results

Cleavage kinetics of human mitochondrial RNase P and contribution of its non-nuclease subunits

View ORCID ProfileElisa Vilardo, Ursula Toth, Enxhi Hazisllari, View ORCID ProfileWalter Rossmanith
doi: https://doi.org/10.1101/2023.03.27.534089
Elisa Vilardo
Center for Anatomy & Cell Biology, Medical University of Vienna, 1090 Vienna, Austria
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Elisa Vilardo
Ursula Toth
Center for Anatomy & Cell Biology, Medical University of Vienna, 1090 Vienna, Austria
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Enxhi Hazisllari
Center for Anatomy & Cell Biology, Medical University of Vienna, 1090 Vienna, Austria
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Walter Rossmanith
Center for Anatomy & Cell Biology, Medical University of Vienna, 1090 Vienna, Austria
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Walter Rossmanith
  • For correspondence: walter.rossmanith@meduniwien.ac.at
  • Abstract
  • Full Text
  • Info/History
  • Metrics
  • Preview PDF
Loading

ABSTRACT

RNase P is the endonuclease responsible for the 5’-end processing of tRNA precursors (pre-tRNAs). Unlike the single-subunit protein-only RNase P (PRORP) found in plants or protists, human mitochondrial RNase P is a multi-enzyme assembly that in addition to the homologous PRORP subunit comprises a methyltransferase (TRMT10C) and a dehydrogenase (SDR5C1) subunit; these proteins, but not their enzymatic activities, are required for efficient pre-tRNA cleavage. Here we report a detailed kinetic analysis of the cleavage reaction by human PRORP and its interplay with TRMT10C-SDR5C1 using a comprehensive set of mitochondrial pre-tRNAs. Surprisingly, we found that PRORP alone binds pre-tRNAs with nanomolar affinity and can even cleave some of them at reduced efficiency without the other subunits. Thus, the ancient binding mode, involving the tRNA elbow and PRORP’s PPR domain, seems retained by human PRORP, and its metallonuclease domain is in principle correctly folded and functional. Our findings support a model according to which the main function of TRMT10C-SDR5C1 is to direct PRORP’s nuclease domain to the cleavage site, thereby increasing the rate and accuracy of cleavage. Human PRORP’s dependence on the extra tRNA binder appears to have evolved to secure specificity in the cleavage of the structurally degenerating mitochondrial tRNAs.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
Back to top
PreviousNext
Posted March 27, 2023.
Download PDF
Email

Thank you for your interest in spreading the word about bioRxiv.

NOTE: Your email address is requested solely to identify you as the sender of this article.

Enter multiple addresses on separate lines or separate them with commas.
Cleavage kinetics of human mitochondrial RNase P and contribution of its non-nuclease subunits
(Your Name) has forwarded a page to you from bioRxiv
(Your Name) thought you would like to see this page from the bioRxiv website.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Share
Cleavage kinetics of human mitochondrial RNase P and contribution of its non-nuclease subunits
Elisa Vilardo, Ursula Toth, Enxhi Hazisllari, Walter Rossmanith
bioRxiv 2023.03.27.534089; doi: https://doi.org/10.1101/2023.03.27.534089
Reddit logo Twitter logo Facebook logo LinkedIn logo Mendeley logo
Citation Tools
Cleavage kinetics of human mitochondrial RNase P and contribution of its non-nuclease subunits
Elisa Vilardo, Ursula Toth, Enxhi Hazisllari, Walter Rossmanith
bioRxiv 2023.03.27.534089; doi: https://doi.org/10.1101/2023.03.27.534089

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Subject Area

  • Biochemistry
Subject Areas
All Articles
  • Animal Behavior and Cognition (4383)
  • Biochemistry (9601)
  • Bioengineering (7097)
  • Bioinformatics (24868)
  • Biophysics (12621)
  • Cancer Biology (9959)
  • Cell Biology (14358)
  • Clinical Trials (138)
  • Developmental Biology (7954)
  • Ecology (12110)
  • Epidemiology (2067)
  • Evolutionary Biology (15989)
  • Genetics (10929)
  • Genomics (14745)
  • Immunology (9871)
  • Microbiology (23680)
  • Molecular Biology (9486)
  • Neuroscience (50884)
  • Paleontology (369)
  • Pathology (1540)
  • Pharmacology and Toxicology (2683)
  • Physiology (4019)
  • Plant Biology (8657)
  • Scientific Communication and Education (1510)
  • Synthetic Biology (2397)
  • Systems Biology (6439)
  • Zoology (1346)