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Proteomic analysis of the U1 snRNP of Schizosaccharomyces pombe reveals three essential organism-specific proteins

Characterization of spliceosomal complexes in the fission yeast Schizosaccharomyces pombe revealed particles sedimenting in the range of 30–60S, exclusively containing U1 snRNA. Here, we report the tandem affinity purification (TAP) of U1-specific protein complexes. The components of the complexes w...

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Autores principales: Newo, Alain N. S., Lützelberger, Martin, Bottner, Claudia A., Wehland, Jürgen, Wissing, Josef, Jänsch, Lothar, Käufer, Norbert F.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1865046/
https://www.ncbi.nlm.nih.gov/pubmed/17264129
http://dx.doi.org/10.1093/nar/gkl1144
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author Newo, Alain N. S.
Lützelberger, Martin
Bottner, Claudia A.
Wehland, Jürgen
Wissing, Josef
Jänsch, Lothar
Käufer, Norbert F.
author_facet Newo, Alain N. S.
Lützelberger, Martin
Bottner, Claudia A.
Wehland, Jürgen
Wissing, Josef
Jänsch, Lothar
Käufer, Norbert F.
author_sort Newo, Alain N. S.
collection PubMed
description Characterization of spliceosomal complexes in the fission yeast Schizosaccharomyces pombe revealed particles sedimenting in the range of 30–60S, exclusively containing U1 snRNA. Here, we report the tandem affinity purification (TAP) of U1-specific protein complexes. The components of the complexes were identified using (LC-MS/MS) mass spectrometry. The fission yeast U1 snRNP contains 16 proteins, including the 7 Sm snRNP core proteins. In both fission and budding yeast, the U1 snRNP contains 9 and 10 U1 specific proteins, respectively, whereas the U1 particle found in mammalian cells contains only 3. Among the U1-specific proteins in S. pombe, three are homolog to the mammalian and six to the budding yeast Saccharomyces cerevisiae U1-specific proteins, whereas three, called U1H, U1J and U1L, are proteins specific to S. pombe. Furthermore, we demonstrate that the homolog of U1-70K and the three proteins specific to S. pombe are essential for growth. We will discuss the differences between the U1 snRNPs with respect to the organism-specific proteins found in the two yeasts and the resulting effect it has on pre-mRNA splicing.
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spelling pubmed-18650462007-05-22 Proteomic analysis of the U1 snRNP of Schizosaccharomyces pombe reveals three essential organism-specific proteins Newo, Alain N. S. Lützelberger, Martin Bottner, Claudia A. Wehland, Jürgen Wissing, Josef Jänsch, Lothar Käufer, Norbert F. Nucleic Acids Res Molecular Biology Characterization of spliceosomal complexes in the fission yeast Schizosaccharomyces pombe revealed particles sedimenting in the range of 30–60S, exclusively containing U1 snRNA. Here, we report the tandem affinity purification (TAP) of U1-specific protein complexes. The components of the complexes were identified using (LC-MS/MS) mass spectrometry. The fission yeast U1 snRNP contains 16 proteins, including the 7 Sm snRNP core proteins. In both fission and budding yeast, the U1 snRNP contains 9 and 10 U1 specific proteins, respectively, whereas the U1 particle found in mammalian cells contains only 3. Among the U1-specific proteins in S. pombe, three are homolog to the mammalian and six to the budding yeast Saccharomyces cerevisiae U1-specific proteins, whereas three, called U1H, U1J and U1L, are proteins specific to S. pombe. Furthermore, we demonstrate that the homolog of U1-70K and the three proteins specific to S. pombe are essential for growth. We will discuss the differences between the U1 snRNPs with respect to the organism-specific proteins found in the two yeasts and the resulting effect it has on pre-mRNA splicing. Oxford University Press 2007-03 2007-01-30 /pmc/articles/PMC1865046/ /pubmed/17264129 http://dx.doi.org/10.1093/nar/gkl1144 Text en © 2007 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Molecular Biology
Newo, Alain N. S.
Lützelberger, Martin
Bottner, Claudia A.
Wehland, Jürgen
Wissing, Josef
Jänsch, Lothar
Käufer, Norbert F.
Proteomic analysis of the U1 snRNP of Schizosaccharomyces pombe reveals three essential organism-specific proteins
title Proteomic analysis of the U1 snRNP of Schizosaccharomyces pombe reveals three essential organism-specific proteins
title_full Proteomic analysis of the U1 snRNP of Schizosaccharomyces pombe reveals three essential organism-specific proteins
title_fullStr Proteomic analysis of the U1 snRNP of Schizosaccharomyces pombe reveals three essential organism-specific proteins
title_full_unstemmed Proteomic analysis of the U1 snRNP of Schizosaccharomyces pombe reveals three essential organism-specific proteins
title_short Proteomic analysis of the U1 snRNP of Schizosaccharomyces pombe reveals three essential organism-specific proteins
title_sort proteomic analysis of the u1 snrnp of schizosaccharomyces pombe reveals three essential organism-specific proteins
topic Molecular Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1865046/
https://www.ncbi.nlm.nih.gov/pubmed/17264129
http://dx.doi.org/10.1093/nar/gkl1144
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