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The yeast THO complex forms a 5-subunit assembly that directly interacts with active chromatin.

Gewartowski K, Cuéllar J, Dziembowski A, Valpuesta JM - Bioarchitecture (2012)

Bottom Line: Recent data indicates that the THO complex is necessary for the proper expression of some genes, assurance of genetic stability by preventing transcription-associated recombination.We discuss the consequences of THO interaction with nucleic acids through the unfolded C-terminal region of Tho2, highlighting the importance of unfolded regions in eukaryotic proteins.Finally, we comment on THO recruitment to active chromatin, a role that is linked to mRNA biogenesis.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biochemistry and Biophysics; Polish Academy of Sciences; Warsaw, Poland; Department of Genetics and Biotechnology; Faculty of Biology; University of Warsaw; Warsaw, Poland.

ABSTRACT
The THO complex is a nuclear structure whose architecture is conserved among all kingdoms and plays an important role in mRNP biogenesis connecting transcription elongation with mRNA maturation and export. Recent data indicates that the THO complex is necessary for the proper expression of some genes, assurance of genetic stability by preventing transcription-associated recombination. Yeast THO has been described as a heterotetramer (Tho2, Hpr1, Mft1 and Thp2) that performs several functions through the interaction with other proteins like Tex1 or the mRNA export factors Sub2 and Yra1, with which it forms the TRanscription and EXport complex (TREX). In this article we review the cellular role of THO, which we show to be composed of five subunits with Tex1 being also an integral part of the complex. We also show a low-resolution structure of THO and localize some of its components. We discuss the consequences of THO interaction with nucleic acids through the unfolded C-terminal region of Tho2, highlighting the importance of unfolded regions in eukaryotic proteins. Finally, we comment on THO recruitment to active chromatin, a role that is linked to mRNA biogenesis.

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Figure 2. Three-dimensional structure of THO, generated by electron microscopy and image processing. The THO complex (EMD-2053) comprises Tho2, Hpr1, Mft1,Thp2 and Tex1 proteins. Different electron microscopy experiments have helped to localized Hpr1, Tex1 and the C-terminal region of Tho2, which is involved in nucleic acid binding [and which we show here in close relation with the RNA polymerase (EMD-1322)]. The localization of the rest of the subunits is speculative.
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Figure 2: Figure 2. Three-dimensional structure of THO, generated by electron microscopy and image processing. The THO complex (EMD-2053) comprises Tho2, Hpr1, Mft1,Thp2 and Tex1 proteins. Different electron microscopy experiments have helped to localized Hpr1, Tex1 and the C-terminal region of Tho2, which is involved in nucleic acid binding [and which we show here in close relation with the RNA polymerase (EMD-1322)]. The localization of the rest of the subunits is speculative.

Mentions: THO was purified using a TAP-tagged Tho214 and this consistently rendered a very pure and stable complex composed of stoichiometric amounts of the four proteins already described as THO components (Tho2, Hpr1, Mft1 and Thp2) and a fifth protein, Tex1. This indicates that THO is a hetero-pentameric complex. The three-dimensional reconstruction of THO,15 performed by electron microscopy and image processing, revealed a long and conspicuous structure with two lateral protrusions (Fig. 2). The resolution of the reconstruction (17 Å) is not good enough to locate the five subunits within the envelope of the complex, so other approaches were used to map some of the components.


The yeast THO complex forms a 5-subunit assembly that directly interacts with active chromatin.

Gewartowski K, Cuéllar J, Dziembowski A, Valpuesta JM - Bioarchitecture (2012)

Figure 2. Three-dimensional structure of THO, generated by electron microscopy and image processing. The THO complex (EMD-2053) comprises Tho2, Hpr1, Mft1,Thp2 and Tex1 proteins. Different electron microscopy experiments have helped to localized Hpr1, Tex1 and the C-terminal region of Tho2, which is involved in nucleic acid binding [and which we show here in close relation with the RNA polymerase (EMD-1322)]. The localization of the rest of the subunits is speculative.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3675074&req=5

Figure 2: Figure 2. Three-dimensional structure of THO, generated by electron microscopy and image processing. The THO complex (EMD-2053) comprises Tho2, Hpr1, Mft1,Thp2 and Tex1 proteins. Different electron microscopy experiments have helped to localized Hpr1, Tex1 and the C-terminal region of Tho2, which is involved in nucleic acid binding [and which we show here in close relation with the RNA polymerase (EMD-1322)]. The localization of the rest of the subunits is speculative.
Mentions: THO was purified using a TAP-tagged Tho214 and this consistently rendered a very pure and stable complex composed of stoichiometric amounts of the four proteins already described as THO components (Tho2, Hpr1, Mft1 and Thp2) and a fifth protein, Tex1. This indicates that THO is a hetero-pentameric complex. The three-dimensional reconstruction of THO,15 performed by electron microscopy and image processing, revealed a long and conspicuous structure with two lateral protrusions (Fig. 2). The resolution of the reconstruction (17 Å) is not good enough to locate the five subunits within the envelope of the complex, so other approaches were used to map some of the components.

Bottom Line: Recent data indicates that the THO complex is necessary for the proper expression of some genes, assurance of genetic stability by preventing transcription-associated recombination.We discuss the consequences of THO interaction with nucleic acids through the unfolded C-terminal region of Tho2, highlighting the importance of unfolded regions in eukaryotic proteins.Finally, we comment on THO recruitment to active chromatin, a role that is linked to mRNA biogenesis.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biochemistry and Biophysics; Polish Academy of Sciences; Warsaw, Poland; Department of Genetics and Biotechnology; Faculty of Biology; University of Warsaw; Warsaw, Poland.

ABSTRACT
The THO complex is a nuclear structure whose architecture is conserved among all kingdoms and plays an important role in mRNP biogenesis connecting transcription elongation with mRNA maturation and export. Recent data indicates that the THO complex is necessary for the proper expression of some genes, assurance of genetic stability by preventing transcription-associated recombination. Yeast THO has been described as a heterotetramer (Tho2, Hpr1, Mft1 and Thp2) that performs several functions through the interaction with other proteins like Tex1 or the mRNA export factors Sub2 and Yra1, with which it forms the TRanscription and EXport complex (TREX). In this article we review the cellular role of THO, which we show to be composed of five subunits with Tex1 being also an integral part of the complex. We also show a low-resolution structure of THO and localize some of its components. We discuss the consequences of THO interaction with nucleic acids through the unfolded C-terminal region of Tho2, highlighting the importance of unfolded regions in eukaryotic proteins. Finally, we comment on THO recruitment to active chromatin, a role that is linked to mRNA biogenesis.

Show MeSH
Related in: MedlinePlus