The LARP6 La module from Tetrabaena socialis reveals structural and functional differences from plant and animal LARP6 homologues
This study identified the LARP6 La Module from Tetrabaena socialis (T. socialis), a four-celled green algae, in an effort to better understand the evolution of LARP6 structure and RNA-binding activity in multicellular eukaryotes. Using a combination of sequence alignments, domain boundary screens, a...
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| Language: | English |
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Taylor & Francis Group
2025-12-01
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| Series: | RNA Biology |
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| Online Access: | https://www.tandfonline.com/doi/10.1080/15476286.2025.2489303 |
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| author | Emily M. Lewis Olga Becker Alexis N. Symons Cora LaCoss A. Jasmine Baclig Avery Guzman Charles Sanders Leticia Gonzalez Lisa R. Warner Karen A. Lewis |
| author_facet | Emily M. Lewis Olga Becker Alexis N. Symons Cora LaCoss A. Jasmine Baclig Avery Guzman Charles Sanders Leticia Gonzalez Lisa R. Warner Karen A. Lewis |
| author_sort | Emily M. Lewis |
| collection | DOAJ |
| description | This study identified the LARP6 La Module from Tetrabaena socialis (T. socialis), a four-celled green algae, in an effort to better understand the evolution of LARP6 structure and RNA-binding activity in multicellular eukaryotes. Using a combination of sequence alignments, domain boundary screens, and structural modelling, we recombinantly expressed and isolated the TsLARP6 La Module to > 98% purity for in vitro biochemical characterization. The La Module is stably folded and exerts minimal RNA binding activity against single-stranded homopolymeric RNAs. Surprisingly, it exhibits low micromolar binding affinity for the vertebrate LARP6 cognate ligand, a bulged-stem loop found in the 5’UTR of collagen type I mRNA, but does not bind double-stranded RNAs of similar size. These result suggests that the TsLARP6 La Module may prefer structured RNA ligands. In contrast, however, the TsLARP6 La Module does not exhibit the RNA chaperone activity that is observed in vertebrate homologs. Therefore, we conclude that protist LARP6 may have both distinct RNA ligands and binding mechanisms from the previously characterized LARP6 proteins of animals and vascular plants, thus establishing a distinct third class of the LARP6 protein family. |
| format | Article |
| id | doaj-art-e9e49fb3f05a4b718d20c87c69f85627 |
| institution | OA Journals |
| issn | 1547-6286 1555-8584 |
| language | English |
| publishDate | 2025-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | RNA Biology |
| spelling | doaj-art-e9e49fb3f05a4b718d20c87c69f856272025-08-20T02:08:35ZengTaylor & Francis GroupRNA Biology1547-62861555-85842025-12-012211910.1080/15476286.2025.2489303The LARP6 La module from Tetrabaena socialis reveals structural and functional differences from plant and animal LARP6 homologuesEmily M. Lewis0Olga Becker1Alexis N. Symons2Cora LaCoss3A. Jasmine Baclig4Avery Guzman5Charles Sanders6Leticia Gonzalez7Lisa R. Warner8Karen A. Lewis9Department of Chemistry and Biochemistry, Texas State University, San Marcos, TX, USADepartment of Chemistry and Biochemistry, Texas State University, San Marcos, TX, USADepartment of Chemistry and Biochemistry, Texas State University, San Marcos, TX, USADepartment of Chemistry and Biochemistry, Texas State University, San Marcos, TX, USADepartment of Chemistry and Biochemistry, Boise State University, Boise, ID, USADepartment of Chemistry and Biochemistry, Texas State University, San Marcos, TX, USADepartment of Chemistry and Biochemistry, Texas State University, San Marcos, TX, USADepartment of Chemistry and Biochemistry, Texas State University, San Marcos, TX, USADepartment of Chemistry and Biochemistry, Boise State University, Boise, ID, USADepartment of Chemistry and Biochemistry, Texas State University, San Marcos, TX, USAThis study identified the LARP6 La Module from Tetrabaena socialis (T. socialis), a four-celled green algae, in an effort to better understand the evolution of LARP6 structure and RNA-binding activity in multicellular eukaryotes. Using a combination of sequence alignments, domain boundary screens, and structural modelling, we recombinantly expressed and isolated the TsLARP6 La Module to > 98% purity for in vitro biochemical characterization. The La Module is stably folded and exerts minimal RNA binding activity against single-stranded homopolymeric RNAs. Surprisingly, it exhibits low micromolar binding affinity for the vertebrate LARP6 cognate ligand, a bulged-stem loop found in the 5’UTR of collagen type I mRNA, but does not bind double-stranded RNAs of similar size. These result suggests that the TsLARP6 La Module may prefer structured RNA ligands. In contrast, however, the TsLARP6 La Module does not exhibit the RNA chaperone activity that is observed in vertebrate homologs. Therefore, we conclude that protist LARP6 may have both distinct RNA ligands and binding mechanisms from the previously characterized LARP6 proteins of animals and vascular plants, thus establishing a distinct third class of the LARP6 protein family.https://www.tandfonline.com/doi/10.1080/15476286.2025.2489303La-related proteinLARPLARP6RNA binding proteinalgaeprotist |
| spellingShingle | Emily M. Lewis Olga Becker Alexis N. Symons Cora LaCoss A. Jasmine Baclig Avery Guzman Charles Sanders Leticia Gonzalez Lisa R. Warner Karen A. Lewis The LARP6 La module from Tetrabaena socialis reveals structural and functional differences from plant and animal LARP6 homologues RNA Biology La-related protein LARP LARP6 RNA binding protein algae protist |
| title | The LARP6 La module from Tetrabaena socialis reveals structural and functional differences from plant and animal LARP6 homologues |
| title_full | The LARP6 La module from Tetrabaena socialis reveals structural and functional differences from plant and animal LARP6 homologues |
| title_fullStr | The LARP6 La module from Tetrabaena socialis reveals structural and functional differences from plant and animal LARP6 homologues |
| title_full_unstemmed | The LARP6 La module from Tetrabaena socialis reveals structural and functional differences from plant and animal LARP6 homologues |
| title_short | The LARP6 La module from Tetrabaena socialis reveals structural and functional differences from plant and animal LARP6 homologues |
| title_sort | larp6 la module from tetrabaena socialis reveals structural and functional differences from plant and animal larp6 homologues |
| topic | La-related protein LARP LARP6 RNA binding protein algae protist |
| url | https://www.tandfonline.com/doi/10.1080/15476286.2025.2489303 |
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