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Telomerase is a ribonucleoprotein enzyme. It adds specific telomeric DNA repeats to the 3'ends of linear chromosomes.  
Telomerase is a ribonucleoprotein enzyme. It adds specific telomeric DNA repeats to the 3'ends of linear chromosomes.  
It was discovered in 1985 by Freider and Blackburn in ''Tetrahymena''. Basically the Telomerase includes an '''RNA (TR) subunit''' and a subunit called '''Telomerase Reverse Transcriptase (TERT)'''. The function of the '''TR''' subunit is to provide the template for telomeric DNA synthesis, which is done by the TERT.
It was discovered in 1985 by Freider and Blackburn in ''Tetrahymena''. Basically the Telomerase includes an '''RNA (TR) subunit''' and a subunit called '''Telomerase Reverse Transcriptase (TERT)'''. The function of the '''TR''' subunit is to provide the template for telomeric DNA synthesis, which is done by the TERT.
The structure of TERT is similar to other reverse transcriptases in their catalytic domain. In contrast to other reverse transcriptases the TERTs have a large N-terminal extension which is called '''TERT essential N-terminal (TEN) domain'''.
The structure of TERT is similar to other reverse transcriptases in their catalytic domain. In contrast to other reverse transcriptases the TERTs have a large N-terminal extension which is called '''TERT essential N-terminal (TEN) domain'''. <PMID: 16462747>
TEN form stable interactions with the telomerase RNA (TR) subunit.
TEN form stable interactions with the telomerase RNA (TR) subunit.
Binding of the RNA subunit is possible, because of the presence of TEN in TERTs.
Binding of the RNA subunit is possible, because of the presence of TEN in TERTs.
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Development of cancer chemotherapeutics directed against the reverse-transcriptase domain of telomerase has been challenging, perhaps because the enzyme needs only low activity to maintain telomeres.
Development of cancer chemotherapeutics directed against the reverse-transcriptase domain of telomerase has been challenging, perhaps because the enzyme needs only low activity to maintain telomeres.
Because the TEN domain is essential for telomerase activity and its structure seems to be conserved trough evolution, this portion of TERT is a potential new target for antitelomerase compounds.
Because the TEN domain is essential for telomerase activity and its structure seems to be conserved trough evolution, this portion of TERT is a potential new target for antitelomerase compounds.
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== '''References''' ==
== '''References''' ==


Informations
<references/>
 
Jacobs SA, Podell ER, Cech TR. Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase Nat Struct Mol Biol. 2006 Mar;13(3):218-25. Epub 2006 Feb 5. Erratum in: Nat Struct Mol Biol. 2007 Oct;14(10):984. PMID: 16462747 [PubMed - indexed for MEDLINE]
 
PDB
 
http://www.pdb.org/pdb/explore/explore.do?structureId=2B2A
 
 
 
<ref>  pmid : 1234567</ref>
 
</references>


==User contributions==
==User contributions==


This page was created with content taken from a page by [[User:Tanja Emmerich]] and [[User:Vinzenz Alejandro Bayro Kaiser]].
This page was created with content taken from a page by [[User:Tanja Emmerich]] and [[User:Vinzenz Alejandro Bayro Kaiser]].

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Eran Hodis, David Canner, Michal Harel, Alexander Berchansky
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