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2h2x

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(New page: 200px<br /><applet load="2h2x" size="350" color="white" frame="true" align="right" spinBox="true" caption="2h2x" /> '''Solution structure of the Tetrahymena telome...)
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==Overview==
==Overview==
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Tetrahymena telomerase RNA (TER) contains several regions in addition to, the template that are important for function. Central among these is the, stem-loop IV domain, which is involved in both catalysis and RNP assembly, and includes binding sites for both the holoenzyme assembly protein p65, and telomerase reverse transcriptase (TERT). Stem-loop IV contains two, regions with high evolutionary sequence conservation: a central GA bulge, between helices, and a terminal loop. We solved the solution structure of, loop IV and modeled the structure of the helical region containing the GA, bulge, using NMR and residual dipolar couplings. The central GA bulge with, flanking C-G base pairs induces a approximately 50 degrees semi-rigid bend, in the helix. Loop IV is highly structured, and contains a conserved C-U, base pair at the top of the helical stem. Analysis of new and previous, biochemical data in light of the structure provides a rationale for some, of the sequence conservation in this region of TER. The results suggest, that during holoenzyme assembly the protein p65 recognizes a bend in stem, IV, and this binding to central stem IV helps to position the structured, loop IV for interaction with TERT and other region(s) of TER.
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Tetrahymena telomerase RNA (TER) contains several regions in addition to the template that are important for function. Central among these is the stem-loop IV domain, which is involved in both catalysis and RNP assembly, and includes binding sites for both the holoenzyme assembly protein p65 and telomerase reverse transcriptase (TERT). Stem-loop IV contains two regions with high evolutionary sequence conservation: a central GA bulge between helices, and a terminal loop. We solved the solution structure of loop IV and modeled the structure of the helical region containing the GA bulge, using NMR and residual dipolar couplings. The central GA bulge with flanking C-G base pairs induces a approximately 50 degrees semi-rigid bend in the helix. Loop IV is highly structured, and contains a conserved C-U base pair at the top of the helical stem. Analysis of new and previous biochemical data in light of the structure provides a rationale for some of the sequence conservation in this region of TER. The results suggest that during holoenzyme assembly the protein p65 recognizes a bend in stem IV, and this binding to central stem IV helps to position the structured loop IV for interaction with TERT and other region(s) of TER.
==About this Structure==
==About this Structure==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Collins, K.]]
[[Category: Collins, K.]]
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[[Category: Connor, C.M.O.]]
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[[Category: Connor, C M.O.]]
[[Category: Feigon, J.]]
[[Category: Feigon, J.]]
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[[Category: Richards, R.J.]]
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[[Category: Richards, R J.]]
[[Category: Trantirek, L.]]
[[Category: Trantirek, L.]]
[[Category: Wu, H.]]
[[Category: Wu, H.]]
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[[Category: heptaloop]]
[[Category: heptaloop]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:13:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:42 2008''

Revision as of 15:37, 21 February 2008

Image:2h2x.gif

2h2x

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Solution structure of the Tetrahymena telomerase RNA stem IV terminal loop

Overview

Tetrahymena telomerase RNA (TER) contains several regions in addition to the template that are important for function. Central among these is the stem-loop IV domain, which is involved in both catalysis and RNP assembly, and includes binding sites for both the holoenzyme assembly protein p65 and telomerase reverse transcriptase (TERT). Stem-loop IV contains two regions with high evolutionary sequence conservation: a central GA bulge between helices, and a terminal loop. We solved the solution structure of loop IV and modeled the structure of the helical region containing the GA bulge, using NMR and residual dipolar couplings. The central GA bulge with flanking C-G base pairs induces a approximately 50 degrees semi-rigid bend in the helix. Loop IV is highly structured, and contains a conserved C-U base pair at the top of the helical stem. Analysis of new and previous biochemical data in light of the structure provides a rationale for some of the sequence conservation in this region of TER. The results suggest that during holoenzyme assembly the protein p65 recognizes a bend in stem IV, and this binding to central stem IV helps to position the structured loop IV for interaction with TERT and other region(s) of TER.

About this Structure

2H2X is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Structural study of elements of Tetrahymena telomerase RNA stem-loop IV domain important for function., Richards RJ, Wu H, Trantirek L, O'Connor CM, Collins K, Feigon J, RNA. 2006 Aug;12(8):1475-85. Epub 2006 Jun 29. PMID:16809815

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