Biochemical Studies Provide Insights into the Necessity for Multiple Arabidopsis thaliana Protein-Only RNase P Isoenzymes.
PRORP
molecular dynamics
substrate recognition
tRNA maturation
temperature–activity profiles
Journal
Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R
Informations de publication
Date de publication:
01 02 2019
01 02 2019
Historique:
received:
19
08
2018
revised:
22
10
2018
accepted:
04
11
2018
pubmed:
12
11
2018
medline:
3
3
2020
entrez:
12
11
2018
Statut:
ppublish
Résumé
RNase P catalyzes removal of the 5' leader from precursor tRNAs (pre-tRNAs) in all three domains of life. Some eukaryotic cells contain multiple forms of the protein-only RNase P (PRORP) variant, prompting efforts to unravel this seeming redundancy. Previous studies concluded that there were only modest differences in the processing of typical pre-tRNAs by the three isoforms in Arabidopsis thaliana [AtPRORP1 (organellar), AtPRORP2 and AtPRORP3 (nuclear)]. Here, we investigated if different physical attributes of the three isoforms might engender payoffs under specific conditions. Our temperature-activity profiling studies revealed that AtPRORPs display substrate-identity dependent behavior at elevated temperatures (37-45 °C), with the organellar variant outperforming the nuclear counterparts. Echoing these findings, molecular dynamics simulations revealed that AtPRORP2 relative to AtPRORP1 samples a wider conformational ensemble that deviates from the crystal structure. Results from our biochemical studies and molecular dynamics simulations support the idea that AtPRORPs have overlapping but not necessarily redundant attributes and inspire new perspectives on the suitability of each variant to perform its function(s) in a specific cellular locale.
Identifiants
pubmed: 30414965
pii: S0022-2836(18)30974-4
doi: 10.1016/j.jmb.2018.11.004
pmc: PMC6349523
mid: NIHMS1511981
pii:
doi:
Substances chimiques
Arabidopsis Proteins
0
Isoenzymes
0
RNA Precursors
0
RNA, Transfer
9014-25-9
Ribonuclease P
EC 3.1.26.5
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
615-624Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM120582
Pays : United States
Organisme : NIH HHS
ID : S10 OD023582
Pays : United States
Informations de copyright
Copyright © 2018 Elsevier Ltd. All rights reserved.
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