An ancient type of MnmA protein is an iron-sulfur cluster-dependent sulfurtransferase for tRNA anticodons.
Identifieur interne : 000177 ( Main/Exploration ); précédent : 000176; suivant : 000178An ancient type of MnmA protein is an iron-sulfur cluster-dependent sulfurtransferase for tRNA anticodons.
Auteurs : Naoki Shigi [Japon] ; Masaki Horitani [Japon] ; Kenjyo Miyauchi [Japon] ; Tsutomu Suzuki [Japon] ; Misao Kuroki [Japon]Source :
- RNA (New York, N.Y.) [ 1469-9001 ] ; 2020.
Descripteurs français
- KwdFr :
- 4-Thiouridine (analogues et dérivés), 4-Thiouridine (métabolisme), ARN de transfert (génétique), Acide glutamique (génétique), Anticodon (génétique), Codon (génétique), Cyanobactéries (génétique), Escherichia coli (génétique), Fer (métabolisme), Glutamine (génétique), Lysine (génétique), Mycobacterium (génétique), Protéines Escherichia coli (génétique), Soufre (métabolisme), Sulfurtransferases (composition chimique), Sulfurtransferases (génétique).
- MESH :
- analogues et dérivés : 4-Thiouridine.
- composition chimique : Sulfurtransferases.
- génétique : ARN de transfert, Acide glutamique, Anticodon, Codon, Cyanobactéries, Escherichia coli, Glutamine, Lysine, Mycobacterium, Protéines Escherichia coli, Sulfurtransferases.
- métabolisme : 4-Thiouridine, Fer, Soufre.
English descriptors
- KwdEn :
- Anticodon (genetics), Codon (genetics), Cyanobacteria (genetics), Escherichia coli (genetics), Escherichia coli Proteins (genetics), Glutamic Acid (genetics), Glutamine (genetics), Iron (metabolism), Lysine (genetics), Mycobacterium (genetics), RNA, Transfer (genetics), Sulfur (metabolism), Sulfurtransferases (chemistry), Sulfurtransferases (genetics), Thiouridine (analogs & derivatives), Thiouridine (metabolism).
- MESH :
- chemical , analogs & derivatives : Thiouridine.
- chemical , chemistry : Sulfurtransferases.
- chemical , genetics : Anticodon, Codon, Escherichia coli Proteins, Glutamic Acid, Glutamine, Lysine, RNA, Transfer, Sulfurtransferases.
- genetics : Cyanobacteria, Escherichia coli, Mycobacterium.
- chemical , metabolism : Iron, Sulfur, Thiouridine.
Abstract
Transfer RNA (tRNA) is an adaptor molecule indispensable for assigning amino acids to codons on mRNA during protein synthesis. 2-thiouridine (s2U) derivatives in the anticodons (position 34) of tRNAs for glutamate, glutamine, and lysine are post-transcriptional modifications essential for precise and efficient codon recognition in all organisms. s2U34 is introduced either by (i) bacterial MnmA/eukaryote mitochondrial Mtu1 or (ii) eukaryote cytosolic Ncs6/archaeal NcsA, and the latter enzymes possess iron-sulfur (Fe-S) cluster. Here, we report the identification of novel-type MnmA homologs containing three conserved Cys residues, which could support Fe-S cluster binding and catalysis, in a broad range of bacteria, including thermophiles, Cyanobacteria, Mycobacteria, Actinomyces, Clostridium, and Helicobacter Using EPR spectroscopy, we revealed that Thermus thermophilus MnmA (TtMnmA) contains an oxygen-sensitive [4Fe-4S]-type cluster. Efficient in vitro formation of s2U34 in tRNALys and tRNAGln by holo-TtMnmA occurred only under anaerobic conditions. Mutational analysis of TtMnmA suggested that the Fe-S cluster is coordinated by the three conserved Cys residues (Cys105, Cys108, and Cys200), and is essential for its activity. Evolutionary scenarios for the sulfurtransferases, including the Fe-S cluster containing Ncs6/NcsA s2U thiouridylases and several distantly related sulfurtransferases, are proposed.
DOI: 10.1261/rna.072066.119
PubMed: 31801798
PubMed Central: PMC7025502
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anticodon (genetics)</term>
<term>Codon (genetics)</term>
<term>Cyanobacteria (genetics)</term>
<term>Escherichia coli (genetics)</term>
<term>Escherichia coli Proteins (genetics)</term>
<term>Glutamic Acid (genetics)</term>
<term>Glutamine (genetics)</term>
<term>Iron (metabolism)</term>
<term>Lysine (genetics)</term>
<term>Mycobacterium (genetics)</term>
<term>RNA, Transfer (genetics)</term>
<term>Sulfur (metabolism)</term>
<term>Sulfurtransferases (chemistry)</term>
<term>Sulfurtransferases (genetics)</term>
<term>Thiouridine (analogs & derivatives)</term>
<term>Thiouridine (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>4-Thiouridine (analogues et dérivés)</term>
<term>4-Thiouridine (métabolisme)</term>
<term>ARN de transfert (génétique)</term>
<term>Acide glutamique (génétique)</term>
<term>Anticodon (génétique)</term>
<term>Codon (génétique)</term>
<term>Cyanobactéries (génétique)</term>
<term>Escherichia coli (génétique)</term>
<term>Fer (métabolisme)</term>
<term>Glutamine (génétique)</term>
<term>Lysine (génétique)</term>
<term>Mycobacterium (génétique)</term>
<term>Protéines Escherichia coli (génétique)</term>
<term>Soufre (métabolisme)</term>
<term>Sulfurtransferases (composition chimique)</term>
<term>Sulfurtransferases (génétique)</term>
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<term>Codon</term>
<term>Escherichia coli Proteins</term>
<term>Glutamic Acid</term>
<term>Glutamine</term>
<term>Lysine</term>
<term>RNA, Transfer</term>
<term>Sulfurtransferases</term>
</keywords>
<keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>4-Thiouridine</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Sulfurtransferases</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Cyanobacteria</term>
<term>Escherichia coli</term>
<term>Mycobacterium</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ARN de transfert</term>
<term>Acide glutamique</term>
<term>Anticodon</term>
<term>Codon</term>
<term>Cyanobactéries</term>
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<term>Glutamine</term>
<term>Lysine</term>
<term>Mycobacterium</term>
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<term>Sulfurtransferases</term>
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<term>Sulfur</term>
<term>Thiouridine</term>
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<term>Fer</term>
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<front><div type="abstract" xml:lang="en">Transfer RNA (tRNA) is an adaptor molecule indispensable for assigning amino acids to codons on mRNA during protein synthesis. 2-thiouridine (s<sup>2</sup>
U) derivatives in the anticodons (position 34) of tRNAs for glutamate, glutamine, and lysine are post-transcriptional modifications essential for precise and efficient codon recognition in all organisms. s<sup>2</sup>
U34 is introduced either by (i) bacterial MnmA/eukaryote mitochondrial Mtu1 or (ii) eukaryote cytosolic Ncs6/archaeal NcsA, and the latter enzymes possess iron-sulfur (Fe-S) cluster. Here, we report the identification of novel-type MnmA homologs containing three conserved Cys residues, which could support Fe-S cluster binding and catalysis, in a broad range of bacteria, including thermophiles, <i>Cyanobacteria</i>
, <i>Mycobacteria</i>
, <i>Actinomyces</i>
, <i>Clostridium</i>
, and <i>Helicobacter</i>
Using EPR spectroscopy, we revealed that <i>Thermus thermophilus</i>
MnmA (TtMnmA) contains an oxygen-sensitive [4Fe-4S]-type cluster. Efficient in vitro formation of s<sup>2</sup>
U34 in tRNA<sup>Lys</sup>
and tRNA<sup>Gln</sup>
by holo-TtMnmA occurred only under anaerobic conditions. Mutational analysis of TtMnmA suggested that the Fe-S cluster is coordinated by the three conserved Cys residues (Cys105, Cys108, and Cys200), and is essential for its activity. Evolutionary scenarios for the sulfurtransferases, including the Fe-S cluster containing Ncs6/NcsA s<sup>2</sup>
U thiouridylases and several distantly related sulfurtransferases, are proposed.</div>
</front>
</TEI>
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<DateCompleted><Year>2020</Year>
<Month>06</Month>
<Day>19</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>06</Month>
<Day>19</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1469-9001</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>26</Volume>
<Issue>3</Issue>
<PubDate><Year>2020</Year>
<Month>03</Month>
</PubDate>
</JournalIssue>
<Title>RNA (New York, N.Y.)</Title>
<ISOAbbreviation>RNA</ISOAbbreviation>
</Journal>
<ArticleTitle>An ancient type of MnmA protein is an iron-sulfur cluster-dependent sulfurtransferase for tRNA anticodons.</ArticleTitle>
<Pagination><MedlinePgn>240-250</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1261/rna.072066.119</ELocationID>
<Abstract><AbstractText>Transfer RNA (tRNA) is an adaptor molecule indispensable for assigning amino acids to codons on mRNA during protein synthesis. 2-thiouridine (s<sup>2</sup>
U) derivatives in the anticodons (position 34) of tRNAs for glutamate, glutamine, and lysine are post-transcriptional modifications essential for precise and efficient codon recognition in all organisms. s<sup>2</sup>
U34 is introduced either by (i) bacterial MnmA/eukaryote mitochondrial Mtu1 or (ii) eukaryote cytosolic Ncs6/archaeal NcsA, and the latter enzymes possess iron-sulfur (Fe-S) cluster. Here, we report the identification of novel-type MnmA homologs containing three conserved Cys residues, which could support Fe-S cluster binding and catalysis, in a broad range of bacteria, including thermophiles, <i>Cyanobacteria</i>
, <i>Mycobacteria</i>
, <i>Actinomyces</i>
, <i>Clostridium</i>
, and <i>Helicobacter</i>
Using EPR spectroscopy, we revealed that <i>Thermus thermophilus</i>
MnmA (TtMnmA) contains an oxygen-sensitive [4Fe-4S]-type cluster. Efficient in vitro formation of s<sup>2</sup>
U34 in tRNA<sup>Lys</sup>
and tRNA<sup>Gln</sup>
by holo-TtMnmA occurred only under anaerobic conditions. Mutational analysis of TtMnmA suggested that the Fe-S cluster is coordinated by the three conserved Cys residues (Cys105, Cys108, and Cys200), and is essential for its activity. Evolutionary scenarios for the sulfurtransferases, including the Fe-S cluster containing Ncs6/NcsA s<sup>2</sup>
U thiouridylases and several distantly related sulfurtransferases, are proposed.</AbstractText>
<CopyrightInformation>© 2020 Shigi et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shigi</LastName>
<ForeName>Naoki</ForeName>
<Initials>N</Initials>
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<Author ValidYN="Y"><LastName>Horitani</LastName>
<ForeName>Masaki</ForeName>
<Initials>M</Initials>
<Identifier Source="ORCID">0000-0002-8881-0600</Identifier>
<AffiliationInfo><Affiliation>Faculty of Agriculture, Department of Applied Biochemistry and Food Science, Saga University, 1 Honjo-machi, Saga 840-8502, Japan.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Miyauchi</LastName>
<ForeName>Kenjyo</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Suzuki</LastName>
<ForeName>Tsutomu</ForeName>
<Initials>T</Initials>
<Identifier Source="ORCID">0000-0002-9731-1731</Identifier>
<AffiliationInfo><Affiliation>Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kuroki</LastName>
<ForeName>Misao</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Biotechnology Research Institute for Drug Discovery, National Institute of Advanced Industrial Science and Technology (AIST), 2-4-7 Aomi, Koto-ku, Tokyo 135-0064, Japan.</Affiliation>
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<Month>12</Month>
<Day>04</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>RNA</MedlineTA>
<NlmUniqueID>9509184</NlmUniqueID>
<ISSNLinking>1355-8382</ISSNLinking>
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<NameOfSubstance UI="C105273">2-thiouridine</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000926">Anticodon</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
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</Chemical>
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<Chemical><RegistryNumber>0RH81L854J</RegistryNumber>
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</Chemical>
<Chemical><RegistryNumber>13957-31-8</RegistryNumber>
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</Chemical>
<Chemical><RegistryNumber>3KX376GY7L</RegistryNumber>
<NameOfSubstance UI="D018698">Glutamic Acid</NameOfSubstance>
</Chemical>
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<Chemical><RegistryNumber>9014-25-9</RegistryNumber>
<NameOfSubstance UI="D012343">RNA, Transfer</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>E1UOL152H7</RegistryNumber>
<NameOfSubstance UI="D007501">Iron</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.1.1.61</RegistryNumber>
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</MeshHeading>
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