Identification and characterization of a putative telomere end-binding protein from Tetrahymena thermophila

dc.contributor.author Dobbs, Drena
dc.contributor.author Sheng, Hong
dc.contributor.author Hou, Zhen
dc.contributor.author Schierer, Ted
dc.contributor.author Henderson, Eric
dc.contributor.author Dobbs, Drena
dc.contributor.author Henderson, Eric
dc.contributor.department Zoology and Genetics
dc.date 2018-02-18T05:05:41.000
dc.date.accessioned 2020-07-07T05:16:46Z
dc.date.available 2020-07-07T05:16:46Z
dc.date.copyright Sun Jan 01 00:00:00 UTC 1995
dc.date.issued 1995-03-01
dc.description.abstract <p>Telomeric DNA of Tetrahymena thermophila consists of a long stretch of (TTGGGG)n double-stranded repeats with a single-stranded (TTGGGG)2 3' overhang at the end of the chromosome. We have identified and characterized a protein that specifically binds to a synthetic telomeric substrate consisting of duplex DNA and the 3' telomeric repeat overhang. This protein is called TEP (telomere end-binding protein). A change from G to A in the third position of the TTGGGG overhang repeat converts the substrate to a human telomere analog and reduces the binding affinity approximately threefold. Changing two G's to C's in the TTGGGG repeats totally abolishes binding. However, permutation of the Tetrahymena repeat sequence has only a minor effect on binding. A duplex structure adjacent to the 3' overhang is required for binding, although the duplex need not contain telomeric repeats. TEP does not bind to G-quartet DNA, which is formed by many G-rich sequences. TEP has a greatly reduced affinity for RNA substrates. The copy number of TEP is at least 2 x 10(4) per cell, and it is present under different conditions of cell growth and development, although its level varies. UV cross-linking experiments show that TEP has an apparent molecular mass of approximately 65 kDa. Unlike other telomere end-binding proteins, TEP is sensitive to high salt concentrations.</p>
dc.description.comments <p>This article is from <em>Molecular and Cellular Biology </em>15 (1995): 1144, doi: <a href="http://dx.doi.org/10.1128/MCB.15.3.1144" target="_blank">10.1128/MCB.15.3.1144</a>. Posted with permission.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/zool_pubs/14/
dc.identifier.articleid 1010
dc.identifier.contextkey 9761215
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath zool_pubs/14
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/92622
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/zool_pubs/14/1995_Dobbs_IdentificationCharacterization.pdf|||Fri Jan 14 20:09:27 UTC 2022
dc.source.uri 10.1128/MCB.15.3.1144
dc.subject.disciplines Cell Biology
dc.subject.disciplines Developmental Biology
dc.subject.disciplines Genetics
dc.subject.disciplines Genomics
dc.subject.disciplines Zoology
dc.title Identification and characterization of a putative telomere end-binding protein from Tetrahymena thermophila
dc.type article
dc.type.genre article
dspace.entity.type Publication
relation.isAuthorOfPublication 7e096c4f-9007-41e4-9414-989c3ea9bc88
relation.isAuthorOfPublication 68bc511a-afd6-4353-ae20-066de33682b9
relation.isOrgUnitOfPublication 4a2929da-5374-4338-b62f-f5fd9e156ef9
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