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Crystal structure of human Acinus RNA recognition motif domain
Acinus is an abundant nuclear protein involved in apoptosis and splicing. It has been implicated in inducing apoptotic chromatin condensation and DNA fragmentation during programmed cell death. Acinus undergoes activation by proteolytic cleavage that produces a truncated p17 form that comprises only...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
PeerJ Inc.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6057467/ https://www.ncbi.nlm.nih.gov/pubmed/30042883 http://dx.doi.org/10.7717/peerj.5163 |
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author | Fernandes, Humberto Czapinska, Honorata Grudziaz, Katarzyna Bujnicki, Janusz M. Nowacka, Martyna |
author_facet | Fernandes, Humberto Czapinska, Honorata Grudziaz, Katarzyna Bujnicki, Janusz M. Nowacka, Martyna |
author_sort | Fernandes, Humberto |
collection | PubMed |
description | Acinus is an abundant nuclear protein involved in apoptosis and splicing. It has been implicated in inducing apoptotic chromatin condensation and DNA fragmentation during programmed cell death. Acinus undergoes activation by proteolytic cleavage that produces a truncated p17 form that comprises only the RNA recognition motif (RRM) domain. We have determined the crystal structure of the human Acinus RRM domain (AcRRM) at 1.65 Å resolution. It shows a classical four-stranded antiparallel β-sheet fold with two flanking α-helices and an additional, non-classical α-helix at the C-terminus, which harbors the caspase-3 target sequence that is cleaved during Acinus activation. In the structure, the C-terminal α-helix partially occludes the potential ligand binding surface of the β-sheet and hypothetically shields it from non-sequence specific interactions with RNA. Based on the comparison with other RRM-RNA complex structures, it is likely that the C-terminal α-helix changes its conformation with respect to the RRM core in order to enable RNA binding by Acinus. |
format | Online Article Text |
id | pubmed-6057467 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | PeerJ Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-60574672018-07-24 Crystal structure of human Acinus RNA recognition motif domain Fernandes, Humberto Czapinska, Honorata Grudziaz, Katarzyna Bujnicki, Janusz M. Nowacka, Martyna PeerJ Biochemistry Acinus is an abundant nuclear protein involved in apoptosis and splicing. It has been implicated in inducing apoptotic chromatin condensation and DNA fragmentation during programmed cell death. Acinus undergoes activation by proteolytic cleavage that produces a truncated p17 form that comprises only the RNA recognition motif (RRM) domain. We have determined the crystal structure of the human Acinus RRM domain (AcRRM) at 1.65 Å resolution. It shows a classical four-stranded antiparallel β-sheet fold with two flanking α-helices and an additional, non-classical α-helix at the C-terminus, which harbors the caspase-3 target sequence that is cleaved during Acinus activation. In the structure, the C-terminal α-helix partially occludes the potential ligand binding surface of the β-sheet and hypothetically shields it from non-sequence specific interactions with RNA. Based on the comparison with other RRM-RNA complex structures, it is likely that the C-terminal α-helix changes its conformation with respect to the RRM core in order to enable RNA binding by Acinus. PeerJ Inc. 2018-07-04 /pmc/articles/PMC6057467/ /pubmed/30042883 http://dx.doi.org/10.7717/peerj.5163 Text en © 2018 Fernandes et al. http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited. |
spellingShingle | Biochemistry Fernandes, Humberto Czapinska, Honorata Grudziaz, Katarzyna Bujnicki, Janusz M. Nowacka, Martyna Crystal structure of human Acinus RNA recognition motif domain |
title | Crystal structure of human Acinus RNA recognition motif domain |
title_full | Crystal structure of human Acinus RNA recognition motif domain |
title_fullStr | Crystal structure of human Acinus RNA recognition motif domain |
title_full_unstemmed | Crystal structure of human Acinus RNA recognition motif domain |
title_short | Crystal structure of human Acinus RNA recognition motif domain |
title_sort | crystal structure of human acinus rna recognition motif domain |
topic | Biochemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6057467/ https://www.ncbi.nlm.nih.gov/pubmed/30042883 http://dx.doi.org/10.7717/peerj.5163 |
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