Circularization restores signal recognition particle RNA functionality in Thermoproteus
Signal recognition particles (SRPs) are universal ribonucleoprotein complexes found in all three domains of life that direct the cellular traffic and secretion of proteins. These complexes consist of SRP proteins and a single, highly structured SRP RNA. Canonical SRP RNA genes have not been identifi...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2015-10-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/11623 |
| _version_ | 1818019718403981312 |
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| author | André Plagens Michael Daume Julia Wiegel Lennart Randau |
| author_facet | André Plagens Michael Daume Julia Wiegel Lennart Randau |
| author_sort | André Plagens |
| collection | DOAJ |
| description | Signal recognition particles (SRPs) are universal ribonucleoprotein complexes found in all three domains of life that direct the cellular traffic and secretion of proteins. These complexes consist of SRP proteins and a single, highly structured SRP RNA. Canonical SRP RNA genes have not been identified for some Thermoproteus species even though they contain SRP19 and SRP54 proteins. Here, we show that genome rearrangement events in Thermoproteus tenax created a permuted SRP RNA gene. The 5'- and 3'-termini of this SRP RNA are located close to a functionally important loop present in all known SRP RNAs. RNA-Seq analyses revealed that these termini are ligated together to generate circular SRP RNA molecules that can bind to SRP19 and SRP54. The circularization site is processed by the tRNA splicing endonuclease. This moonlighting activity of the tRNA splicing machinery permits the permutation of the SRP RNA and creates highly stable and functional circular RNA molecules. |
| first_indexed | 2024-04-14T07:56:03Z |
| format | Article |
| id | doaj.art-d3b0635485644fb6a7b51cab5bc58c5c |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-14T07:56:03Z |
| publishDate | 2015-10-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-d3b0635485644fb6a7b51cab5bc58c5c2022-12-22T02:05:03ZengeLife Sciences Publications LtdeLife2050-084X2015-10-01410.7554/eLife.11623Circularization restores signal recognition particle RNA functionality in ThermoproteusAndré Plagens0Michael Daume1Julia Wiegel2Lennart Randau3Max Planck Institute for Terrestrial Microbiology, Marburg, GermanyMax Planck Institute for Terrestrial Microbiology, Marburg, GermanyMax Planck Institute for Terrestrial Microbiology, Marburg, GermanyMax Planck Institute for Terrestrial Microbiology, Marburg, Germany; LOEWE Center for Synthetic Microbiology, Synmikro, Marburg, GermanySignal recognition particles (SRPs) are universal ribonucleoprotein complexes found in all three domains of life that direct the cellular traffic and secretion of proteins. These complexes consist of SRP proteins and a single, highly structured SRP RNA. Canonical SRP RNA genes have not been identified for some Thermoproteus species even though they contain SRP19 and SRP54 proteins. Here, we show that genome rearrangement events in Thermoproteus tenax created a permuted SRP RNA gene. The 5'- and 3'-termini of this SRP RNA are located close to a functionally important loop present in all known SRP RNAs. RNA-Seq analyses revealed that these termini are ligated together to generate circular SRP RNA molecules that can bind to SRP19 and SRP54. The circularization site is processed by the tRNA splicing endonuclease. This moonlighting activity of the tRNA splicing machinery permits the permutation of the SRP RNA and creates highly stable and functional circular RNA molecules.https://elifesciences.org/articles/11623Thermoproteus tenaxRNA processingsplicingarchaeasignal recognition particle |
| spellingShingle | André Plagens Michael Daume Julia Wiegel Lennart Randau Circularization restores signal recognition particle RNA functionality in Thermoproteus eLife Thermoproteus tenax RNA processing splicing archaea signal recognition particle |
| title | Circularization restores signal recognition particle RNA functionality in Thermoproteus |
| title_full | Circularization restores signal recognition particle RNA functionality in Thermoproteus |
| title_fullStr | Circularization restores signal recognition particle RNA functionality in Thermoproteus |
| title_full_unstemmed | Circularization restores signal recognition particle RNA functionality in Thermoproteus |
| title_short | Circularization restores signal recognition particle RNA functionality in Thermoproteus |
| title_sort | circularization restores signal recognition particle rna functionality in thermoproteus |
| topic | Thermoproteus tenax RNA processing splicing archaea signal recognition particle |
| url | https://elifesciences.org/articles/11623 |
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