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The sole LSm complex in Cyanidioschyzon merolae associates with pre-mRNA splicing and mRNA degradation factors

Proteins of the Sm and Sm-like (LSm) families, referred to collectively as (L)Sm proteins, are found in all three domains of life and are known to promote a variety of RNA processes such as base-pair formation, unwinding, RNA degradation, and RNA stabilization. In eukaryotes, (L)Sm proteins have bee...

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Autores principales: Reimer, Kirsten A., Stark, Martha R., Aguilar, Lisbeth-Carolina, Stark, Sierra R., Burke, Robert D., Moore, Jack, Fahlman, Richard P., Yip, Calvin K., Kuroiwa, Haruko, Oeffinger, Marlene, Rader, Stephen D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5435867/
https://www.ncbi.nlm.nih.gov/pubmed/28325844
http://dx.doi.org/10.1261/rna.058487.116
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author Reimer, Kirsten A.
Stark, Martha R.
Aguilar, Lisbeth-Carolina
Stark, Sierra R.
Burke, Robert D.
Moore, Jack
Fahlman, Richard P.
Yip, Calvin K.
Kuroiwa, Haruko
Oeffinger, Marlene
Rader, Stephen D.
author_facet Reimer, Kirsten A.
Stark, Martha R.
Aguilar, Lisbeth-Carolina
Stark, Sierra R.
Burke, Robert D.
Moore, Jack
Fahlman, Richard P.
Yip, Calvin K.
Kuroiwa, Haruko
Oeffinger, Marlene
Rader, Stephen D.
author_sort Reimer, Kirsten A.
collection PubMed
description Proteins of the Sm and Sm-like (LSm) families, referred to collectively as (L)Sm proteins, are found in all three domains of life and are known to promote a variety of RNA processes such as base-pair formation, unwinding, RNA degradation, and RNA stabilization. In eukaryotes, (L)Sm proteins have been studied, inter alia, for their role in pre-mRNA splicing. In many organisms, the LSm proteins form two distinct complexes, one consisting of LSm1–7 that is involved in mRNA degradation in the cytoplasm, and the other consisting of LSm2–8 that binds spliceosomal U6 snRNA in the nucleus. We recently characterized the splicing proteins from the red alga Cyanidioschyzon merolae and found that it has only seven LSm proteins. The identities of CmLSm2–CmLSm7 were unambiguous, but the seventh protein was similar to LSm1 and LSm8. Here, we use in vitro binding measurements, microscopy, and affinity purification-mass spectrometry to demonstrate a canonical splicing function for the C. merolae LSm complex and experimentally validate our bioinformatic predictions of a reduced spliceosome in this organism. Copurification of Pat1 and its associated mRNA degradation proteins with the LSm proteins, along with evidence of a cytoplasmic fraction of CmLSm complexes, argues that this complex is involved in both splicing and cytoplasmic mRNA degradation. Intriguingly, the Pat1 complex also copurifies with all four snRNAs, suggesting the possibility of a spliceosome-associated pre-mRNA degradation complex in the nucleus.
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spelling pubmed-54358672018-06-01 The sole LSm complex in Cyanidioschyzon merolae associates with pre-mRNA splicing and mRNA degradation factors Reimer, Kirsten A. Stark, Martha R. Aguilar, Lisbeth-Carolina Stark, Sierra R. Burke, Robert D. Moore, Jack Fahlman, Richard P. Yip, Calvin K. Kuroiwa, Haruko Oeffinger, Marlene Rader, Stephen D. RNA Article Proteins of the Sm and Sm-like (LSm) families, referred to collectively as (L)Sm proteins, are found in all three domains of life and are known to promote a variety of RNA processes such as base-pair formation, unwinding, RNA degradation, and RNA stabilization. In eukaryotes, (L)Sm proteins have been studied, inter alia, for their role in pre-mRNA splicing. In many organisms, the LSm proteins form two distinct complexes, one consisting of LSm1–7 that is involved in mRNA degradation in the cytoplasm, and the other consisting of LSm2–8 that binds spliceosomal U6 snRNA in the nucleus. We recently characterized the splicing proteins from the red alga Cyanidioschyzon merolae and found that it has only seven LSm proteins. The identities of CmLSm2–CmLSm7 were unambiguous, but the seventh protein was similar to LSm1 and LSm8. Here, we use in vitro binding measurements, microscopy, and affinity purification-mass spectrometry to demonstrate a canonical splicing function for the C. merolae LSm complex and experimentally validate our bioinformatic predictions of a reduced spliceosome in this organism. Copurification of Pat1 and its associated mRNA degradation proteins with the LSm proteins, along with evidence of a cytoplasmic fraction of CmLSm complexes, argues that this complex is involved in both splicing and cytoplasmic mRNA degradation. Intriguingly, the Pat1 complex also copurifies with all four snRNAs, suggesting the possibility of a spliceosome-associated pre-mRNA degradation complex in the nucleus. Cold Spring Harbor Laboratory Press 2017-06 /pmc/articles/PMC5435867/ /pubmed/28325844 http://dx.doi.org/10.1261/rna.058487.116 Text en © 2017 Reimer et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.
spellingShingle Article
Reimer, Kirsten A.
Stark, Martha R.
Aguilar, Lisbeth-Carolina
Stark, Sierra R.
Burke, Robert D.
Moore, Jack
Fahlman, Richard P.
Yip, Calvin K.
Kuroiwa, Haruko
Oeffinger, Marlene
Rader, Stephen D.
The sole LSm complex in Cyanidioschyzon merolae associates with pre-mRNA splicing and mRNA degradation factors
title The sole LSm complex in Cyanidioschyzon merolae associates with pre-mRNA splicing and mRNA degradation factors
title_full The sole LSm complex in Cyanidioschyzon merolae associates with pre-mRNA splicing and mRNA degradation factors
title_fullStr The sole LSm complex in Cyanidioschyzon merolae associates with pre-mRNA splicing and mRNA degradation factors
title_full_unstemmed The sole LSm complex in Cyanidioschyzon merolae associates with pre-mRNA splicing and mRNA degradation factors
title_short The sole LSm complex in Cyanidioschyzon merolae associates with pre-mRNA splicing and mRNA degradation factors
title_sort sole lsm complex in cyanidioschyzon merolae associates with pre-mrna splicing and mrna degradation factors
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5435867/
https://www.ncbi.nlm.nih.gov/pubmed/28325844
http://dx.doi.org/10.1261/rna.058487.116
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