Evidence map›Paper›PMID 36614280›Full record

ArticleInternational journal of molecular sciences2023

Quick and Spontaneous Transformation between [3Fe-4S] and [4Fe-4S] Iron-Sulfur Clusters in the tRNA-Thiolation Enzyme TtuA.

Masato Ishizaka, Minghao Chen, Shun Narai, Yoshikazu Tanaka, Toyoyuki Ose, Masaki Horitani, Min Yao

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Masato IshizakaGraduate School of Life Science, Hokkaido University, Kita 8, Nishi 5, Kita-ku, Sapporo 060-0810, Japan.ORCID 0000-0003-0906-5209
Minghao ChenFaculty of Advanced Life Science, Hokkaido University, Kita 8, Nishi 5, Kita-ku, Sapporo 060-0810, Japan.
Shun NaraiGraduate School of Life Science, Hokkaido University, Kita 8, Nishi 5, Kita-ku, Sapporo 060-0810, Japan.
Yoshikazu TanakaFaculty of Advanced Life Science, Hokkaido University, Kita 8, Nishi 5, Kita-ku, Sapporo 060-0810, Japan.ORCID 0000-0002-7893-3236
Toyoyuki OseGraduate School of Life Science, Hokkaido University, Kita 8, Nishi 5, Kita-ku, Sapporo 060-0810, Japan.
Masaki HoritaniFaculty of Agriculture, Department of Applied Biochemistry and Food Science, Saga University, 1 Honjo-machi, Saga 840-8502, Japan.ORCID 0000-0002-8881-0600
Min YaoGraduate School of Life Science, Hokkaido University, Kita 8, Nishi 5, Kita-ku, Sapporo 060-0810, Japan.ORCID 0000-0003-1687-5904

Funding

Grants-in-Aid for Scientific Research 21J12999Grants-in-Aid for Scientific Research 21K18937Grants-in-Aid for Scientific Research 22H04816Hokkaido University "Ambitious Leader's Program" Z0119000020-002Hokkaido University "Ambitious Leader's Program" B2086000021-001Institute for Molecular Science JPMXP09S21MS1075bJapan Agency for Medical Research and Development JP18am0101071
6 · The paper itself

Abstract

Iron-sulfur (Fe-S) clusters are essential cofactors for enzyme activity. These Fe-S clusters are present in structurally diverse forms, including [4Fe-4S] and [3Fe-4S]. Type-identification of the Fe-S cluster is indispensable in understanding the catalytic mechanism of enzymes. However, identifying [4Fe-4S] and [3Fe-4S] clusters in particular is challenging because of their rapid transformation in response to oxidation-reduction events. In this study, we focused on the relationship between the Fe-S cluster type and the catalytic activity of a tRNA-thiolation enzyme (TtuA). We reconstituted [4Fe-4S]-TtuA, prepared [3Fe-4S]-TtuA by oxidizing [4Fe-4S]-TtuA under strictly anaerobic conditions, and then observed changes in the Fe-S clusters in the samples and the enzymatic activity in the time-course experiments. Electron paramagnetic resonance analysis revealed that [3Fe-4S]-TtuA spontaneously transforms into [4Fe-4S]-TtuA in minutes to one hour without an additional free Fe source in the solution. Although the TtuA immediately after oxidation of [4Fe-4S]-TtuA was inactive [3Fe-4S]-TtuA, its activity recovered to a significant level compared to [4Fe-4S]-TtuA after one hour, corresponding to an increase of [4Fe-4S]-TtuA in the solution. Our findings reveal that [3Fe-4S]-TtuA is highly inactive and unstable. Moreover, time-course analysis of structural changes and activity under strictly anaerobic conditions further unraveled the Fe-S cluster type used by the tRNA-thiolation enzyme.

Indexed as

IronIron-Sulfur ProteinsElectron Spin Resonance SpectroscopyOxidation-ReductionRNA, TransferSulfurIronIron-Sulfur ProteinsRNA, TransferSulfur2-thiouridine biosynthesisEPR spectroscopyiron–sulfur clusterredox biochemistrysulfurtransferasetRNA sulfur modificationtRNA-thiolation

Identifiers

PMID36614280
PMCPMC9821441

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.