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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Main Authors: Jesper Buchhave Poulsen, Lee Edward Sanderson, Emil Dandanell Agerschou, Emil Dedic, Thomas Boesen, Ditlev E Brodersen
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4111604?pdf=render
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spelling 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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