TY - JOUR
T1 - A chlamydomonas protein that binds single-stranded G-strand telomere DNA
AU - Petracek, M. E.
AU - Konkel, L. M.C.
AU - Kable, M. L.
AU - Berman, J.
PY - 1994
Y1 - 1994
N2 - 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), and a cDNA encoding this G-strand binding protein was identified by its expression of a G-strand binding activity. The cDNA (GBPI) 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.
AB - 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), and a cDNA encoding this G-strand binding protein was identified by its expression of a G-strand binding activity. The cDNA (GBPI) 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.
KW - Chlamydomonas telomeres
KW - RNA recognition motif
KW - Single-stranded binding protein
KW - Teleromeric DNA
UR - http://www.scopus.com/inward/record.url?scp=0028169375&partnerID=8YFLogxK
U2 - 10.1002/j.1460-2075.1994.tb06672.x
DO - 10.1002/j.1460-2075.1994.tb06672.x
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AN - SCOPUS:0028169375
SN - 0261-4189
VL - 13
SP - 3648
EP - 3658
JO - EMBO Journal
JF - EMBO Journal
IS - 15
ER -