Telomerase Reverse Transcriptase: Difference between revisions

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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'''. <PMID: 16462747>
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'''. <ref>PMID: 16462747</ref>
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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== '''Experimental fragment with TEN''' ==
== '''Experimental fragment with TEN''' ==


<applet load='2b2a' size='400' frame='true' align='right' caption='Insert caption here' scene='Sandbox/Presentation/3' />
<applet load='2b2a' size='400' frame='true' align='right' caption='Tetrahymena thermophila telomerase reverse transcriptase TEN domain [[2b2a]]' scene='Sandbox/Presentation/3' />
A Tetrahymena Thermophila TERT fragment consisting of residues 2-191 with an N-terminal His6 tag was cristallized in space group P3 with <scene name='Sandbox/Three/1'>three</scene> TERT molecules present in the crystallographic asymmetric unit.  
A Tetrahymena Thermophila TERT fragment consisting of residues 2-191 with an N-terminal His6 tag was cristallized in space group P3 with <scene name='Sandbox/Three/1'>three</scene> TERT molecules present in the crystallographic asymmetric unit.  
This 23.5-kDa fragment contains only one methionine residue, making phasing by substitution with selenomethionine (SeMet) difficult.
This 23.5-kDa fragment contains only one methionine residue, making phasing by substitution with selenomethionine (SeMet) difficult.
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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.
==3D structures of telomerase reverse transcriptase==
See [[Telomerase]]
=='''Additional Resources'''==
For additional information, See: [[Cancer]]
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== '''References''' ==
== '''References''' ==
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==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 from a page authored by [[User:Tanja Emmerich]] and [[User:Vinzenz Alejandro Bayro Kaiser]].
[[Category:Topic Page]]

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Eran Hodis, David Canner, Michal Harel, Alexander Berchansky