Telomerase
From Proteopedia
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== History == | == History == | ||
| - | In the 1930s, Barbara McClintock was the first to point out that the ends of chromosomes are somewhat different. Over forty years later, Olovnikov (1973) and Watson (1972) indicated an 'end replication problem' in which the lagging strand of DNA cannot be fully copied (Blackburn 2010). This concept led to a waterfall of studies and information vitally important to cellular regulation. In 1978, acclaimed chemist and front-runner in telomerase studies, Elizabeth H. Blackburn, discovered the telomere in ''Tetrahymena thermophila''. By 1985, Blackburn and Carol Greider noted the enzymatic activity that created the telomeric sequences, and in 1987, the two women officially identified the telomerase as a ribonucleaoprotein with an essential RNA and and protein component (Corey 2009). | + | In the 1930s, Barbara McClintock was the first to point out that the ends of chromosomes are somewhat different. Over forty years later, Olovnikov (1973) and Watson (1972) indicated an 'end replication problem' in which the lagging strand of DNA cannot be fully copied (Blackburn 2010). This concept led to a waterfall of studies and information vitally important to cellular regulation. In 1978, acclaimed chemist and front-runner in telomerase studies, Elizabeth H. Blackburn, discovered the telomere in ''Tetrahymena thermophila''. By 1985, Blackburn and Carol Greider noted the enzymatic activity that created the telomeric sequences, and in 1987, the two women officially identified the telomerase as a ribonucleaoprotein with an essential RNA and and protein component (Corey 2009). Elizabeth Blackburn, Carol Greider, and Jack Szostak won the 2009 Noble Prize in Physiology or Medicine for their lifetime work regarding the telomere and telomerase. |
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| + | Since 1987, the study of the telomerase has exploded. [[Image:Figure1.jpg]] | ||
== Structure == | == Structure == | ||
Revision as of 21:00, 13 October 2014
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Contents |
Introduction
The telomerase is a complex composed of an RNA primer and protein that adds repeated DNA sequences to a 3' DNA strand. This ribonucleoprotein acts as a reverse transcriptase that creates a DNA sequence complementary to its RNA primer in its catalytic subunit, TERT. The sequences attached to the end of DNA is non-coding DNA that functions as protection from mutation and degradation. As DNA replications occurs, the polymerase that copies in the 5' to 3' direction, cannot copy the end of the lagging strand which leaves unpaired bases that may code for a specific gene. Multiple unpaired ends can form hydrogen bonds or even swap genetic material. The telomerase fixes this issue and lengthens the strands, because the replication process slowly shortens the ends of chromosomes. This enzyme also plays a role in coordinating cell division. Complementary issues of aging and cancer describe the inactivation or over-activation of telomerase activity.
History
In the 1930s, Barbara McClintock was the first to point out that the ends of chromosomes are somewhat different. Over forty years later, Olovnikov (1973) and Watson (1972) indicated an 'end replication problem' in which the lagging strand of DNA cannot be fully copied (Blackburn 2010). This concept led to a waterfall of studies and information vitally important to cellular regulation. In 1978, acclaimed chemist and front-runner in telomerase studies, Elizabeth H. Blackburn, discovered the telomere in Tetrahymena thermophila. By 1985, Blackburn and Carol Greider noted the enzymatic activity that created the telomeric sequences, and in 1987, the two women officially identified the telomerase as a ribonucleaoprotein with an essential RNA and and protein component (Corey 2009). Elizabeth Blackburn, Carol Greider, and Jack Szostak won the 2009 Noble Prize in Physiology or Medicine for their lifetime work regarding the telomere and telomerase.
Since 1987, the study of the telomerase has exploded. Image:Figure1.jpg
Structure
Active Site Chemistry
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