8gap - Revision history

OCA at 06:48, 19 June 2024

2024-06-19T06:48:53Z

← Older revision		Revision as of 06:48, 19 June 2024
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	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/TERT_TETTS TERT_TETTS] Catalytic component of telomerase, an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER (PubMed:10944124, PubMed:15696174, PubMed:~~17322903~~, PubMed:~~20713447~~, PubMed:~~16462747~~). TERT is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme (PubMed:10944124, PubMed:15696174, PubMed:~~17322903~~, PubMed:~~20713447~~, PubMed:~~16462747~~).<ref>PMID:10944124</ref> <ref>PMID:15696174</ref> <ref>PMID:16462747</ref> <ref>PMID:17322903</ref> <ref>PMID:20713447</ref>		[https://www.uniprot.org/uniprot/TERT_TETTS TERT_TETTS] Catalytic component of telomerase, an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER (PubMed:10944124, PubMed:15696174, PubMed:16462747, PubMed:17322903, PubMed:20713447). TERT is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme (PubMed:10944124, PubMed:15696174, PubMed:16462747, PubMed:17322903, PubMed:20713447).<ref>PMID:10944124</ref> <ref>PMID:15696174</ref> <ref>PMID:16462747</ref> <ref>PMID:17322903</ref> <ref>PMID:20713447</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	La-related protein 7 (LARP7) are a family of RNA chaperones that protect the 3'-end of RNA and are components of specific ribonucleoprotein complexes (RNP). In Tetrahymena thermophila telomerase, LARP7 protein p65 together with telomerase reverse transcriptase (TERT) and telomerase RNA (TER) form the core RNP. p65 has four known domains-N-terminal domain (NTD), La motif (LaM), RNA recognition motif 1 (RRM1), and C-terminal xRRM2. To date, only the xRRM2 and LaM and their interactions with TER have been structurally characterized. Conformational dynamics leading to low resolution in cryo-EM density maps have limited our understanding of how full-length p65 specifically recognizes and remodels TER for telomerase assembly. Here, we combined focused classification of Tetrahymena telomerase cryo-EM maps with NMR spectroscopy to determine the structure of p65-TER. Three previously unknown helices are identified, one in the otherwise intrinsically disordered NTD that binds the La module, one that extends RRM1, and another preceding xRRM2, that stabilize p65-TER interactions. The extended La module (alphaN, LaM and RRM1) interacts with the four 3' terminal U nucleotides, while LaM and alphaN additionally interact with TER pseudoknot, and LaM with stem 1 and 5' end. Our results reveal the extensive p65-TER interactions that promote TER 3'-end protection, TER folding, and core RNP assembly and stabilization. The structure of full-length p65 with TER also sheds light on the biological roles of genuine La and LARP7 proteins as RNA chaperones and core RNP components.

	Structure of LARP7 Protein p65-telomerase RNA Complex in Telomerase Revealed by Cryo-EM and NMR.,Wang Y, He Y, Wang Y, Yang Y, Singh M, Eichhorn CD, Cheng X, Xiao Jiang Y, Hong Zhou Z, Feigon J J Mol Biol. 2023 Mar 20:168044. doi: 10.1016/j.jmb.2023.168044. PMID:37330293<ref>PMID:37330293</ref>		==See Also==
			*[[Telomerase 3D structures\|Telomerase 3D structures]]
	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class~~=~~"pdbe-citations 8gap" style~~=~~"background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:19, 28 June 2023

2023-06-28T21:19:30Z

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-The entry 8gap is ON HOLD  until Paper Publication
+==Structure of LARP7 protein p65-telomerase RNA complex in telomerase==
-Authors:
+Structure of LARP7 Protein p65-telomerase RNA Complex in Telomerase Revealed by Cryo-EM and NMR.,Wang Y, He Y, Wang Y, Yang Y, Singh M, Eichhorn CD, Cheng X, Xiao Jiang Y, Hong Zhou Z, Feigon J J Mol Biol. 2023 Mar 20:168044. doi: 10.1016/j.jmb.2023.168044. PMID:37330293<ref>PMID:37330293</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>

OCA at 07:43, 15 March 2023

2023-03-15T07:43:35Z

← Older revision		Revision as of 07:43, 15 March 2023
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 8gap is ON HOLD		The entry 8gap is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "8gap" [edit=sysop:move=sysop]

2023-03-02T04:34:18Z

Protected "8gap" [edit=sysop:move=sysop]

← Older revision	Revision as of 04:34, 2 March 2023
(No difference)

OCA: New page: '''Unreleased structure''' The entry 8gap is ON HOLD Authors: Description: Category: Unreleased Structures

2023-03-02T04:34:17Z

New page: '''Unreleased structure''' The entry 8gap is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8gap is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]