Sub-Cellular Localization And Complex Formation By Aminoacyl-tRNA Synthetases In Cyanobacteria: Evidence For Interaction Of Membrane-Anchored ValRS With ATP Synthase
tRNAs are charged with cognate amino acids by aminoacyl-tRNA synthetases (aaRSs) and subsequently delivered to the ribosome to be used as substrates for gene translation. Whether aminoacyl-tRNAs are channeled to the ribosome by transit within translational complexes that avoid their diffusion in the...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2016-06-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.00857/full |
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| author | Javier eSantamaría-Gómez Jesús A.G. Ochoa De Alda Elvira eOlmedo-Verd Roque eBru-Martinez Ignacio eLuque |
| author_facet | Javier eSantamaría-Gómez Jesús A.G. Ochoa De Alda Elvira eOlmedo-Verd Roque eBru-Martinez Ignacio eLuque |
| author_sort | Javier eSantamaría-Gómez |
| collection | DOAJ |
| description | tRNAs are charged with cognate amino acids by aminoacyl-tRNA synthetases (aaRSs) and subsequently delivered to the ribosome to be used as substrates for gene translation. Whether aminoacyl-tRNAs are channeled to the ribosome by transit within translational complexes that avoid their diffusion in the cytoplasm is a matter of intense investigation in organisms of the three domains of life. In the cyanobacterium Anabaena sp. PCC 7120, the valyl-tRNA synthetase (ValRS) is anchored to thylakoid membranes by means of the CAAD domain. We have investigated whether in this organism ValRS could act as a hub for the nucleation of a translational complex by attracting other aaRSs to the membranes. Out of the 20 aaRSs, only ValRS was found to localize in thylakoid membranes whereas the other enzymes occupied the soluble portion of the cytoplasm. To investigate the basis for this asymmetric distribution of aaRSs, a global search for proteins interacting with the 20 aaRSs was conducted. The interaction between ValRS and the FoF1 ATP synthase complex here reported is of utmost interest and suggests a functional link between elements of the gene translation and energy production machineries. |
| first_indexed | 2024-04-12T23:29:50Z |
| format | Article |
| id | doaj.art-cb020c2d601b431c90418d9d9f131d70 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-04-12T23:29:50Z |
| publishDate | 2016-06-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-cb020c2d601b431c90418d9d9f131d702022-12-22T03:12:19ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2016-06-01710.3389/fmicb.2016.00857206468Sub-Cellular Localization And Complex Formation By Aminoacyl-tRNA Synthetases In Cyanobacteria: Evidence For Interaction Of Membrane-Anchored ValRS With ATP SynthaseJavier eSantamaría-Gómez0Jesús A.G. Ochoa De Alda1Elvira eOlmedo-Verd2Roque eBru-Martinez3Ignacio eLuque4CSIC and Universidad de SevillaUniversidad de ExtremaduraCSIC and Universidad de SevillaUniversidad de AlicanteCSIC and Universidad de SevillatRNAs are charged with cognate amino acids by aminoacyl-tRNA synthetases (aaRSs) and subsequently delivered to the ribosome to be used as substrates for gene translation. Whether aminoacyl-tRNAs are channeled to the ribosome by transit within translational complexes that avoid their diffusion in the cytoplasm is a matter of intense investigation in organisms of the three domains of life. In the cyanobacterium Anabaena sp. PCC 7120, the valyl-tRNA synthetase (ValRS) is anchored to thylakoid membranes by means of the CAAD domain. We have investigated whether in this organism ValRS could act as a hub for the nucleation of a translational complex by attracting other aaRSs to the membranes. Out of the 20 aaRSs, only ValRS was found to localize in thylakoid membranes whereas the other enzymes occupied the soluble portion of the cytoplasm. To investigate the basis for this asymmetric distribution of aaRSs, a global search for proteins interacting with the 20 aaRSs was conducted. The interaction between ValRS and the FoF1 ATP synthase complex here reported is of utmost interest and suggests a functional link between elements of the gene translation and energy production machineries.http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.00857/fullCyanobacteriaThylakoidsFOF1 ATP synthaseaminoacyl-tRNA synthetasesCAADmembrane-anchoring |
| spellingShingle | Javier eSantamaría-Gómez Jesús A.G. Ochoa De Alda Elvira eOlmedo-Verd Roque eBru-Martinez Ignacio eLuque Sub-Cellular Localization And Complex Formation By Aminoacyl-tRNA Synthetases In Cyanobacteria: Evidence For Interaction Of Membrane-Anchored ValRS With ATP Synthase Frontiers in Microbiology Cyanobacteria Thylakoids FOF1 ATP synthase aminoacyl-tRNA synthetases CAAD membrane-anchoring |
| title | Sub-Cellular Localization And Complex Formation By Aminoacyl-tRNA Synthetases In Cyanobacteria: Evidence For Interaction Of Membrane-Anchored ValRS With ATP Synthase |
| title_full | Sub-Cellular Localization And Complex Formation By Aminoacyl-tRNA Synthetases In Cyanobacteria: Evidence For Interaction Of Membrane-Anchored ValRS With ATP Synthase |
| title_fullStr | Sub-Cellular Localization And Complex Formation By Aminoacyl-tRNA Synthetases In Cyanobacteria: Evidence For Interaction Of Membrane-Anchored ValRS With ATP Synthase |
| title_full_unstemmed | Sub-Cellular Localization And Complex Formation By Aminoacyl-tRNA Synthetases In Cyanobacteria: Evidence For Interaction Of Membrane-Anchored ValRS With ATP Synthase |
| title_short | Sub-Cellular Localization And Complex Formation By Aminoacyl-tRNA Synthetases In Cyanobacteria: Evidence For Interaction Of Membrane-Anchored ValRS With ATP Synthase |
| title_sort | sub cellular localization and complex formation by aminoacyl trna synthetases in cyanobacteria evidence for interaction of membrane anchored valrs with atp synthase |
| topic | Cyanobacteria Thylakoids FOF1 ATP synthase aminoacyl-tRNA synthetases CAAD membrane-anchoring |
| url | http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.00857/full |
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