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2j04

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(New page: 200px<br /><applet load="2j04" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j04, resolution 3.20&Aring;" /> '''THE TAU60-TAU91 SUBC...)
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'''THE TAU60-TAU91 SUBCOMPLEX OF YEAST TRANSCRIPTION FACTOR IIIC'''<br />
'''THE TAU60-TAU91 SUBCOMPLEX OF YEAST TRANSCRIPTION FACTOR IIIC'''<br />
==Overview==
==Overview==
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Yeast RNA polymerase III is recruited upon binding of subcomplexes tauA, and tauB of transcription factor IIIC (TFIIIC) to the A and B blocks of, tRNA gene promoters. The tauB subcomplex consists of subunits tau60, tau91, and tau138. We determined the 3.2 A crystal structure of tau60, bound to a large C-terminal fragment of tau91 (Deltatau91). Deltatau91, protein contains a seven-bladed propeller preceded by an N-terminal, extension, whereas tau60 contains a structurally homologous propeller, followed by a C-terminal domain with a novel alpha/beta fold. The two, propeller domains do not have any detectable DNA binding activity and, mediate heterodimer formation that may serve as scaffold for tau138, assembly. We show that the C-terminal tau60 domain interacts with the TATA, binding protein (TBP). Recombinant tauB recruits TBP and stimulates, TFIIIB-directed transcription on a TATA box containing tRNA gene, implying, a combined contribution of tauA and tauB to preinitiation complex, formation.
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Yeast RNA polymerase III is recruited upon binding of subcomplexes tauA and tauB of transcription factor IIIC (TFIIIC) to the A and B blocks of tRNA gene promoters. The tauB subcomplex consists of subunits tau60, tau91, and tau138. We determined the 3.2 A crystal structure of tau60 bound to a large C-terminal fragment of tau91 (Deltatau91). Deltatau91 protein contains a seven-bladed propeller preceded by an N-terminal extension, whereas tau60 contains a structurally homologous propeller followed by a C-terminal domain with a novel alpha/beta fold. The two propeller domains do not have any detectable DNA binding activity and mediate heterodimer formation that may serve as scaffold for tau138 assembly. We show that the C-terminal tau60 domain interacts with the TATA binding protein (TBP). Recombinant tauB recruits TBP and stimulates TFIIIB-directed transcription on a TATA box containing tRNA gene, implying a combined contribution of tauA and tauB to preinitiation complex formation.
==About this Structure==
==About this Structure==
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2J04 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J04 OCA].
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2J04 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J04 OCA].
==Reference==
==Reference==
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[[Category: Fernandez-Tornero, C.]]
[[Category: Fernandez-Tornero, C.]]
[[Category: Legrand, P.]]
[[Category: Legrand, P.]]
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[[Category: Muller, C.W.]]
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[[Category: Muller, C W.]]
[[Category: Mylona, A.]]
[[Category: Mylona, A.]]
[[Category: beta propeller]]
[[Category: beta propeller]]
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[[Category: yeast rna polymerase iii]]
[[Category: yeast rna polymerase iii]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:30:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:58:01 2008''

Revision as of 15:58, 21 February 2008

Image:2j04.jpg

2j04, resolution 3.20Å

Drag the structure with the mouse to rotate

THE TAU60-TAU91 SUBCOMPLEX OF YEAST TRANSCRIPTION FACTOR IIIC

Overview

Yeast RNA polymerase III is recruited upon binding of subcomplexes tauA and tauB of transcription factor IIIC (TFIIIC) to the A and B blocks of tRNA gene promoters. The tauB subcomplex consists of subunits tau60, tau91, and tau138. We determined the 3.2 A crystal structure of tau60 bound to a large C-terminal fragment of tau91 (Deltatau91). Deltatau91 protein contains a seven-bladed propeller preceded by an N-terminal extension, whereas tau60 contains a structurally homologous propeller followed by a C-terminal domain with a novel alpha/beta fold. The two propeller domains do not have any detectable DNA binding activity and mediate heterodimer formation that may serve as scaffold for tau138 assembly. We show that the C-terminal tau60 domain interacts with the TATA binding protein (TBP). Recombinant tauB recruits TBP and stimulates TFIIIB-directed transcription on a TATA box containing tRNA gene, implying a combined contribution of tauA and tauB to preinitiation complex formation.

About this Structure

2J04 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: insights into preinitiation complex assembly., Mylona A, Fernandez-Tornero C, Legrand P, Haupt M, Sentenac A, Acker J, Muller CW, Mol Cell. 2006 Oct 20;24(2):221-32. PMID:17052456

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