A Novel Aminoacyl-tRNA Synthetase Appended Domain Can Supply the Core Synthetase with Its Amino Acid Substrate
The structural organization and functionality of aminoacyl-tRNA synthetases have been expanded through polypeptide additions to their core aminoacylation domain. We have identified a novel domain appended to the methionyl-tRNA synthetase (MetRS) of the intracellular pathogen Mycoplasma penetrans. Sequence analysis of this N-terminal region suggests the appended domain is an aminotransferase, which we demonstrate here. The aminotransferase domain of MpMetRS is capable of generating methionine from its α-keto acid analog, 2-keto-4-methylthiobutyrate (KMTB). The methionine thus produced can be subsequently attached to cognate tRNAMet in the MpMetRS aminoacylation domain. Genomic erosion in the Mycoplasma species has impaired many canonical biosynthetic pathways, causing them to rely on their host for numerous metabolites. It is still unclear if this bifunctional MetRS is a key part of pathogen life cycle or is a neutral consequence of the reductive evolution experienced by Mycoplasma species.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2020 |
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Erschienen: |
2020 |
Enthalten in: |
Zur Gesamtaufnahme - volume:11 |
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Enthalten in: |
Genes - 11(2020), 11 vom: 07. Nov. |
Sprache: |
Englisch |
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Beteiligte Personen: |
Muraski, Marc [VerfasserIn] |
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Links: |
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Anmerkungen: |
Date Completed 26.07.2021 Date Revised 26.07.2021 published: Electronic Citation Status MEDLINE |
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doi: |
10.3390/genes11111320 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM317393596 |
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100 | 1 | |a Muraski, Marc |e verfasserin |4 aut | |
245 | 1 | 2 | |a A Novel Aminoacyl-tRNA Synthetase Appended Domain Can Supply the Core Synthetase with Its Amino Acid Substrate |
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500 | |a Citation Status MEDLINE | ||
520 | |a The structural organization and functionality of aminoacyl-tRNA synthetases have been expanded through polypeptide additions to their core aminoacylation domain. We have identified a novel domain appended to the methionyl-tRNA synthetase (MetRS) of the intracellular pathogen Mycoplasma penetrans. Sequence analysis of this N-terminal region suggests the appended domain is an aminotransferase, which we demonstrate here. The aminotransferase domain of MpMetRS is capable of generating methionine from its α-keto acid analog, 2-keto-4-methylthiobutyrate (KMTB). The methionine thus produced can be subsequently attached to cognate tRNAMet in the MpMetRS aminoacylation domain. Genomic erosion in the Mycoplasma species has impaired many canonical biosynthetic pathways, causing them to rely on their host for numerous metabolites. It is still unclear if this bifunctional MetRS is a key part of pathogen life cycle or is a neutral consequence of the reductive evolution experienced by Mycoplasma species | ||
650 | 4 | |a Journal Article | |
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700 | 1 | |a Nilsson, Emil |e verfasserin |4 aut | |
700 | 1 | |a Weekley, Benjamin |e verfasserin |4 aut | |
700 | 1 | |a Sharma, Sandhya Bharti |e verfasserin |4 aut | |
700 | 1 | |a Alexander, Rebecca W |e verfasserin |4 aut | |
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