NDLI: TPP1 OB-fold domain controls telomere maintenance by recruiting telomerase to chromosome ends

Content Provider	PubMed Central
Author	Zhong, Franklin L. Batista, Luis F. Z. Freund, Adam Pech, Matthew F. Venteicher, Andrew S. Artandi, Steven E.
Copyright Year	2012
Abstract	Telomere synthesis in cancer cells and stem cells involves trafficking of telomerase to Cajal bodies, and telomerase is thought to be recruited to telomeres through interactions with telomere-binding proteins. Here, we show that the OB-fold domain of the telomere-binding protein TPP1 recruits telomerase to telomeres through an association with the telomerase reverse transcriptase, TERT. When tethered away from telomeres and other telomere-binding proteins, the TPP1 OB-fold domain is sufficient to recruit telomerase to a heterologous chromatin locus. A minimal TPP1 OB-fold serves to inhibit telomere maintenance by blocking access of telomerase to its cognate binding site at telomeres. We identify specific loop residues within the TPP1 OB-fold necessary for association with telomerase, and critical residues in TERT, including those mutated in a subset of pulmonary fibrosis patients. These data define a potential interface for telomerase-TPP1 interaction required for telomere maintenance and implicate defective telomerase recruitment in telomerase-related disease.
Related Links	http://dx.doi.org/10.1016/j.cell.2012.07.012
Ending Page	494
Page Count	14
Starting Page	481
File Format	PDF
ISSN	00928674
e-ISSN	10974172
Journal	Cell
Issue Number	3
Volume Number	150
Language	English
Publisher Date	2012-08-01
Access Restriction	Open
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry, Genetics and Molecular Biology

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Functional interaction between telomere protein TPP1 and telomerase

Ku interacts with telomerase RNA to promote telomere addition at native and broken chromosome ends

OB Fold-containing Protein 1 (OBFC1), a Human Homolog of Yeast Stn1, Associates with TPP1 and Is Implicated in Telomere Length Regulation*

OB Fold-containing Protein 1 (OBFC1), a Human Homolog of Yeast Stn1, Associates with TPP1 and Is Implicated in Telomere Length Regulation

Human UPF1 interacts with TPP1 and telomerase and sustains telomere leading-strand replication

OB Fold Contributes to Telomere Maintenance.

The Est3 protein associates with yeast telomerase through an OB-fold domain

Putative Telomere-Recruiting Domain in the Catalytic Subunit of Human Telomerase

The tenacious recognition of yeast telomere sequence by Cdc13 is fully exerted by a single OB-fold domain

TPP1 OB-fold domain controls telomere maintenance by recruiting telomerase to chromosome ends

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TPP1 OB-fold domain controls telomere maintenance by recruiting telomerase to chromosome ends