Structural characterization of the Saccharomyces cerevisiae THO complex by small-angle X-ray scattering.
The THO complex participates during eukaryotic mRNA biogenesis in coupling transcription to formation and nuclear export of translation-competent messenger ribonucleoprotein particles. In Saccharomyces cerevisiae, THO has been defined as a heteropentamer composed of the Tho2p, Hpr1p, Tex1p, Mft1p, a...
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doaj-b92d3331b2584aeaa2ad2b8c366157a12020-11-25T01:11:09ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0197e10347010.1371/journal.pone.0103470Structural characterization of the Saccharomyces cerevisiae THO complex by small-angle X-ray scattering.Jesper Buchhave PoulsenLee Edward SandersonEmil Dandanell AgerschouEmil DedicThomas BoesenDitlev E BrodersenThe THO complex participates during eukaryotic mRNA biogenesis in coupling transcription to formation and nuclear export of translation-competent messenger ribonucleoprotein particles. In Saccharomyces cerevisiae, THO has been defined as a heteropentamer composed of the Tho2p, Hpr1p, Tex1p, Mft1p, and Thp2p subunits and the overall three-dimensional shape of the complex has been established by negative stain electron microscopy. Here, we use small-angle X-ray scattering measured for isolated THO components (Mft1p and Thp2p) as well as THO subcomplexes (Mft1p-Thp2p and Mft1p-Thp2p-Tho2p) to construct structural building blocks that allow positioning of each subunit within the complex. To accomplish this, the individual envelopes determined for Mft1p and Thp2p are first fitted inside those of the Mft1p-Thp2p and Mft1p-Thp2p-Tho2p complexes. Next, the ternary complex structure is placed in the context of the five-component electron microscopy structure. Our model reveals not only the position of each protein in the THO complex relative to each other, but also shows that the pentamer is likely somewhat larger than what was observed by electron microscopy.http://europepmc.org/articles/PMC4111604?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jesper Buchhave Poulsen Lee Edward Sanderson Emil Dandanell Agerschou Emil Dedic Thomas Boesen Ditlev E Brodersen |
spellingShingle |
Jesper Buchhave Poulsen Lee Edward Sanderson Emil Dandanell Agerschou Emil Dedic Thomas Boesen Ditlev E Brodersen Structural characterization of the Saccharomyces cerevisiae THO complex by small-angle X-ray scattering. PLoS ONE |
author_facet |
Jesper Buchhave Poulsen Lee Edward Sanderson Emil Dandanell Agerschou Emil Dedic Thomas Boesen Ditlev E Brodersen |
author_sort |
Jesper Buchhave Poulsen |
title |
Structural characterization of the Saccharomyces cerevisiae THO complex by small-angle X-ray scattering. |
title_short |
Structural characterization of the Saccharomyces cerevisiae THO complex by small-angle X-ray scattering. |
title_full |
Structural characterization of the Saccharomyces cerevisiae THO complex by small-angle X-ray scattering. |
title_fullStr |
Structural characterization of the Saccharomyces cerevisiae THO complex by small-angle X-ray scattering. |
title_full_unstemmed |
Structural characterization of the Saccharomyces cerevisiae THO complex by small-angle X-ray scattering. |
title_sort |
structural characterization of the saccharomyces cerevisiae tho complex by small-angle x-ray scattering. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2014-01-01 |
description |
The THO complex participates during eukaryotic mRNA biogenesis in coupling transcription to formation and nuclear export of translation-competent messenger ribonucleoprotein particles. In Saccharomyces cerevisiae, THO has been defined as a heteropentamer composed of the Tho2p, Hpr1p, Tex1p, Mft1p, and Thp2p subunits and the overall three-dimensional shape of the complex has been established by negative stain electron microscopy. Here, we use small-angle X-ray scattering measured for isolated THO components (Mft1p and Thp2p) as well as THO subcomplexes (Mft1p-Thp2p and Mft1p-Thp2p-Tho2p) to construct structural building blocks that allow positioning of each subunit within the complex. To accomplish this, the individual envelopes determined for Mft1p and Thp2p are first fitted inside those of the Mft1p-Thp2p and Mft1p-Thp2p-Tho2p complexes. Next, the ternary complex structure is placed in the context of the five-component electron microscopy structure. Our model reveals not only the position of each protein in the THO complex relative to each other, but also shows that the pentamer is likely somewhat larger than what was observed by electron microscopy. |
url |
http://europepmc.org/articles/PMC4111604?pdf=render |
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