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The THO complex as a key mRNP biogenesis factor in development and cell differentiation.

Jimeno S, Aguilera A - J. Biol. (2010)

Bottom Line: The THO complex is a key component in the co-transcriptional formation of messenger ribonucleoparticles that are competent to be exported from the nucleus, yet its precise function is unknown.A recent study in BMC Biology on the role of the THOC5 subunit in cell physiology and mouse development provides new clues to the role of the THO complex in cell differentiation.

View Article: PubMed Central - HTML - PubMed

Affiliation: Centro Andaluz de Biología Molecular y Medicina Regenerativa, Av. Américo Vespucio s/n, 41092 Sevilla, Spain.

ABSTRACT
The THO complex is a key component in the co-transcriptional formation of messenger ribonucleoparticles that are competent to be exported from the nucleus, yet its precise function is unknown. A recent study in BMC Biology on the role of the THOC5 subunit in cell physiology and mouse development provides new clues to the role of the THO complex in cell differentiation.

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The THO complex functions in mRNP biogenesis at the interface between transcription and export of mRNA from the nucleus. Proteins are shown with their yeast name followed by the name of the human homolog, where the two differ, for Nab2, Mtr2/p15, Sub2/UAP56, Mex67/TAP, Yra1/ALY, or with the yeast name followed by the Drosophila name for Sus1/ENY2. Protein complexes are shown in capital letters: THO, THSC (also called TREX-2) and SAGA. Proteins that interact with each other or between which a physical connection has been reported are in the same color. Sus1 can act as a subunit of both THSC and SAGA complexes. Unlabeled proteins in gray represent other factors important for mRNP biogenesis and export. NPC, nuclear pore complex; RNAPII, RNA polymerase II.
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Figure 1: The THO complex functions in mRNP biogenesis at the interface between transcription and export of mRNA from the nucleus. Proteins are shown with their yeast name followed by the name of the human homolog, where the two differ, for Nab2, Mtr2/p15, Sub2/UAP56, Mex67/TAP, Yra1/ALY, or with the yeast name followed by the Drosophila name for Sus1/ENY2. Protein complexes are shown in capital letters: THO, THSC (also called TREX-2) and SAGA. Proteins that interact with each other or between which a physical connection has been reported are in the same color. Sus1 can act as a subunit of both THSC and SAGA complexes. Unlabeled proteins in gray represent other factors important for mRNP biogenesis and export. NPC, nuclear pore complex; RNAPII, RNA polymerase II.

Mentions: As soon as the pre-mRNA has been transcribed from DNA in the nucleus, it is processed into a mature ribonucleoprotein (mRNP) particle, which is competent to be exported from the nucleus. The THO complex, a nuclear protein complex conserved from yeast to humans, is involved in the biogenesis of mRNP particles and functions at the interface between transcription and RNA export (Figure 1).


The THO complex as a key mRNP biogenesis factor in development and cell differentiation.

Jimeno S, Aguilera A - J. Biol. (2010)

The THO complex functions in mRNP biogenesis at the interface between transcription and export of mRNA from the nucleus. Proteins are shown with their yeast name followed by the name of the human homolog, where the two differ, for Nab2, Mtr2/p15, Sub2/UAP56, Mex67/TAP, Yra1/ALY, or with the yeast name followed by the Drosophila name for Sus1/ENY2. Protein complexes are shown in capital letters: THO, THSC (also called TREX-2) and SAGA. Proteins that interact with each other or between which a physical connection has been reported are in the same color. Sus1 can act as a subunit of both THSC and SAGA complexes. Unlabeled proteins in gray represent other factors important for mRNP biogenesis and export. NPC, nuclear pore complex; RNAPII, RNA polymerase II.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2871528&req=5

Figure 1: The THO complex functions in mRNP biogenesis at the interface between transcription and export of mRNA from the nucleus. Proteins are shown with their yeast name followed by the name of the human homolog, where the two differ, for Nab2, Mtr2/p15, Sub2/UAP56, Mex67/TAP, Yra1/ALY, or with the yeast name followed by the Drosophila name for Sus1/ENY2. Protein complexes are shown in capital letters: THO, THSC (also called TREX-2) and SAGA. Proteins that interact with each other or between which a physical connection has been reported are in the same color. Sus1 can act as a subunit of both THSC and SAGA complexes. Unlabeled proteins in gray represent other factors important for mRNP biogenesis and export. NPC, nuclear pore complex; RNAPII, RNA polymerase II.
Mentions: As soon as the pre-mRNA has been transcribed from DNA in the nucleus, it is processed into a mature ribonucleoprotein (mRNP) particle, which is competent to be exported from the nucleus. The THO complex, a nuclear protein complex conserved from yeast to humans, is involved in the biogenesis of mRNP particles and functions at the interface between transcription and RNA export (Figure 1).

Bottom Line: The THO complex is a key component in the co-transcriptional formation of messenger ribonucleoparticles that are competent to be exported from the nucleus, yet its precise function is unknown.A recent study in BMC Biology on the role of the THOC5 subunit in cell physiology and mouse development provides new clues to the role of the THO complex in cell differentiation.

View Article: PubMed Central - HTML - PubMed

Affiliation: Centro Andaluz de Biología Molecular y Medicina Regenerativa, Av. Américo Vespucio s/n, 41092 Sevilla, Spain.

ABSTRACT
The THO complex is a key component in the co-transcriptional formation of messenger ribonucleoparticles that are competent to be exported from the nucleus, yet its precise function is unknown. A recent study in BMC Biology on the role of the THOC5 subunit in cell physiology and mouse development provides new clues to the role of the THO complex in cell differentiation.

Show MeSH
Related in: MedlinePlus