The POT1-TPP1 telomere complex is a telomerase processivity factor
dc.contributor.author | Wang, Feng | en_US |
dc.contributor.author | Podell, Elaine R. | en_US |
dc.contributor.author | Zaug, Arthur J. | en_US |
dc.contributor.author | Yang, Yuting | en_US |
dc.contributor.author | Baciu, Paul | en_US |
dc.contributor.author | Cech, Thomas R. | en_US |
dc.contributor.author | Lei, Ming | en_US |
dc.date.accessioned | 2009-06-01T17:44:53Z | |
dc.date.available | 2009-06-01T17:44:53Z | |
dc.date.issued | 2007-02-01 | en_US |
dc.identifier.citation | Wang, Feng; Podell, Elaine R.; Zaug, Arthur J.; Yang, Yuting; Baciu, Paul; Cech, Thomas R.; Lei, Ming. (2007) "The POT1-TPP1 telomere complex is a telomerase processivity factor." Nature 445(7127): 506-510. <http://hdl.handle.net/2027.42/62923> | en_US |
dc.identifier.issn | 0028-0836 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/62923 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=17237768&dopt=citation | en_US |
dc.description.abstract | Telomeres were originally defined as chromosome caps that prevent the natural ends of linear chromosomes from undergoing deleterious degradation and fusion events. POT1 ( protection of telomeres) protein binds the single-stranded G-rich DNA overhangs at human chromosome ends and suppresses unwanted DNA repair activities. TPP1 is a previously identified binding partner of POT1 that has been proposed to form part of a six-protein shelterin complex at telomeres. Here, the crystal structure of a domain of human TPP1 reveals an oligonucleotide/oligosaccharide-binding fold that is structurally similar to the beta-subunit of the telomere end-binding protein of a ciliated protozoan, suggesting that TPP1 is the missing beta-subunit of human POT1 protein. Telomeric DNA end-binding proteins have generally been found to inhibit rather than stimulate the action of the chromosome end-replicating enzyme, telomerase. In contrast, we find that TPP1 and POT1 form a complex with telomeric DNA that increases the activity and processivity of the human telomerase core enzyme. We propose that POT1 - TPP1 switches from inhibiting telomerase access to the telomere, as a component of shelterin, to serving as a processivity factor for telomerase during telomere extension. | en_US |
dc.format.extent | 1048601 bytes | |
dc.format.extent | 2489 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Nature Publishing Group | en_US |
dc.source | Nature | en_US |
dc.title | The POT1-TPP1 telomere complex is a telomerase processivity factor | en_US |
dc.type | Article | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Univ Michigan, Sch Med, Dept Biol Chem, Ann Arbor, MI 48109 USA | en_US |
dc.contributor.affiliationother | Univ Colorado, Howard Hughes Med Inst, Dept Chem & Biochem, Boulder, CO 80309 USA | en_US |
dc.identifier.pmid | 17237768 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/62923/1/nature05454.pdf | |
dc.identifier.doi | http://dx.doi.org/10.1038/nature05454 | en_US |
dc.identifier.source | Nature | en_US |
dc.contributor.authoremail | leim@umich.edu | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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