| pubmed-article:8062839 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8062839 | lifeskim:mentions | umls-concept:C0008155 | lld:lifeskim |
| pubmed-article:8062839 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:8062839 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8062839 | lifeskim:mentions | umls-concept:C0085187 | lld:lifeskim |
| pubmed-article:8062839 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:8062839 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:8062839 | pubmed:dateCreated | 1994-9-21 | lld:pubmed |
| pubmed-article:8062839 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8062839 | pubmed:abstractText | We have identified a protein in Chlamydomonas reinhardtii cell extracts that specifically binds the single-stranded (ss) Chlamydomonas G-strand telomere sequence (TTTTAGGG)n. This protein, called G-strand binding protein (GBP), binds DNA with two or more ss TTTTAGGG repeats. A single polypeptide (M(r) 34 kDa) in Chlamydomonas extracts binds (TTTTAGGG)n, and a cDNA encoding this G-strand binding protein was identified by its expression of a G-strand binding activity. The cDNA (GBP1) sequence predicts a protein product (Gbp1p) that includes two domains with extensive homology to RNA recognition motifs (RRMs) and a region rich in glycine, alanine and arginine. Antibody raised against a peptide within Gbp1p reacted with both the 34 kDa polypeptide and bound G-strand DNA-protein complexes in gel retardation assays, indicating that GBP1 encodes GBP. Unlike vertebrate heteronuclear ribonucleoproteins, GBP does not bind the cognate telomere RNA sequence UUUUAGGG in gel retardation, North-Western or competition assays. Thus, GBP is a new type of candidate telomere binding protein that binds, in vitro, to ss G-strand telomere DNA, the primer for telomerase, and has domains that have homology to RNA binding domains in other proteins. | lld:pubmed |
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| pubmed-article:8062839 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8062839 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8062839 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8062839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8062839 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8062839 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8062839 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:8062839 | pubmed:author | pubmed-author:BermanJJ | lld:pubmed |
| pubmed-article:8062839 | pubmed:author | pubmed-author:PetracekM EME | lld:pubmed |
| pubmed-article:8062839 | pubmed:author | pubmed-author:KonkelL MLM | lld:pubmed |
| pubmed-article:8062839 | pubmed:author | pubmed-author:LECOQPP | lld:pubmed |
| pubmed-article:8062839 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8062839 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8062839 | pubmed:volume | 13 | lld:pubmed |
