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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1998-4-21
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pubmed:abstractText |
In this work, we have identified and characterized proteins in rice nuclear extracts that specifically bind the single-stranded G-rich telomere sequence. Three types of specific DNA-protein complexes (I, II, and III) were identified by gel retardation assays using synthetic telomere substrates consisting of two or more single-stranded TTTAGGG repeats and rice nuclear extracts. Since each complex has a unique biochemical property and differs in electrophoretic mobility, at least three different proteins interact with the G-rich telomere sequences. These proteins are called rice G-rich telomere binding protein (RGBP) and none of them show binding affinity to double-stranded telomere repeats or single-stranded C-rich sequence. Changing one or two G's to C's in the TTTAGGG repeats abolishes binding activity. RGBPs have a greatly reduced affinity for human and Tetrahymena telomeric sequence and do not efficiently bind the cognate G-rich telomere RNA sequence UUUAGGG. Like other telomere binding proteins, RGBPs are resistant to high salt concentrations. RNase sensitivity of the DNA-protein interaction. In this assay, we observed a novel complex (complex III) in gel retardation assays which did not alter the mobilities or the band intensities of the two pre-existing complexes (I and II). The complex III, in addition to binding to telomeric sequences, has a binding affinity to rice nuclear RNA, whereas two other complexes have a binding affinity to only single-stranded G-rich telomere DNA. Taken together, these studies suggest that RGBPs are new types of telomere-binding proteins that bind in vitro to single-stranded G-rich telomere DNA in the angiosperms.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Single-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotide Probes,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Chloride
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0167-4412
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
36
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
661-72
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9526498-Animals,
pubmed-meshheading:9526498-Base Composition,
pubmed-meshheading:9526498-Base Sequence,
pubmed-meshheading:9526498-Binding Sites,
pubmed-meshheading:9526498-DNA, Single-Stranded,
pubmed-meshheading:9526498-DNA-Binding Proteins,
pubmed-meshheading:9526498-Humans,
pubmed-meshheading:9526498-Oligodeoxyribonucleotides,
pubmed-meshheading:9526498-Oligonucleotide Probes,
pubmed-meshheading:9526498-Oryza sativa,
pubmed-meshheading:9526498-Plant Proteins,
pubmed-meshheading:9526498-Protein Binding,
pubmed-meshheading:9526498-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:9526498-Sodium Chloride,
pubmed-meshheading:9526498-Telomere
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pubmed:year |
1998
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pubmed:articleTitle |
Rice proteins that bind single-stranded G-rich telomere DNA.
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pubmed:affiliation |
Department of Biology, Yonsei University, Seoul, Korea.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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