Sentences with phrase «telomerase rna»

Of the two telomerase components analyzed, Tert (telomerase reverse transcriptase) expression did not show any differences between groups, but Terc (telomerase RNA component) transcription was significantly higher in the IVC testes (Fig. 2B).

To understand how telomerase RNA participates in mechanistic aspects of telomere synthesis, we studied a conserved secondary structure adjacent to the template.

In telomeric DNA mutants of Tetrahymena thermophila, created by expression of a telomerase RNA with an altered template sequence, division of the germline nucleus was severely delayed or blocked in anaphase.

Studies have shown the modification of TERC (TElomerase RNA Component) expression may be therapeutically beneficial in DC patients.

The variant lies near a gene called telomerase RNA component, or TERC, and earlier studies in animals have shown that low TERC expression is associated with shorter telomeres, and faster biological aging.

Researchers chased the gene down and found it was a mutant telomerase RNA gene component, and patients had about half the normal amount of telomerase, which meant their telomeres shorten prematurely.

We used liposomes — which are almost like tiny soap bubbles in the bloodstream — to deliver a gene that knocks the telomerase RNA down.

Amounts of telomerase RNA increased in immortal cells derived from primary mouse fibroblasts.

The mouse telomerase RNA component was cloned and contained only 65 percent sequence identity with the human telomerase RNA.

Not exact matches

Telomerase is a «ribonucleoprotein complex» composed of a protein component and an RNA primer sequence which acts to protect the terminal ends of chromosomes.

Since then, his team has been creating molecular inhibitors to target the TRBD RNA - binding pockets as means to inhibit telomerase enzymatic activity.

«Telomerase is a unique protein - RNA complex where the protein subunit uses its RNA component as a template to add identical fragments of DNA to the end of chromosomes,» said Emmanuel Skordalakes, Ph.D., associate professor in the Gene Expression and Regulation program of Wistar's NCI - designated Cancer Center.

«This TFLY motif comprises a significant part of the binding pocket that enables the enzyme to grapple the RNA template and guide it to the active site of the enzyme for catalysis,» Skordalakes said, «but it also facilitates the stable association of the protein with its RNA component thus forming a fully functional telomerase enzyme.»

This model structure of the catalytic portion of telomerase shows how the TFLY motif (green) is positioned at the entry of the pocket that guides the RNA template in the interior cavity of the telomerase ring and were the active site of the enzyme if located for catalysis.

The RNA binding domain (TRBD) of telomerase is a crucial component to this process and, therefore, the enzyme's ability to work.

According to Skordalakes, one way to do so would be to disrupt the protein RNA complex that comprises the core of the telomerase enzyme.

Within this portion they identified the TFLY, a conserved element that they showed is involved in binding the RNA component of telomerase and this interaction is important for telomerase protein - RNA assembly and activity.

The scientists speculated that when chromosome tips get too stubby — a process that can be reversed by telomerase, an enzyme made up of protein and RNA — cells cease replicating and enter a state called senescence (see» More Than a Sum of Our Cells»).

Greider and Ariel Avilion, a grad student working in her lab toward a Ph.D. from the State University of New York, Stony Brook, were attempting to find and isolate the gene for the RNA portion — dubbed hTR — of human telomerase.

The ribonucleoprotein enzyme telomerase synthesizes telomeric DNA by copying an internal RNA template sequence.

The telomerase ribonucleoprotein has a phylogenetically divergent RNA subunit, which contains a short template for telomeric DNA synthesis.

This study reveals a specific function for an RNA structure in the enzymatic action of telomerase.

Greider, Blackburn and Szostak discovered telomerase, the enzyme that copies the ends of chromosomes using a special RNA template.

NOP2 and NAF1 both interact with DKC1, and all three proteins are required for the stability, correct assembly and intranuclear trafficking of TERC, the RNA component of telomerase.