hnRNP A2/B1 binds specifically to single stranded vertebrate telomeric repeat TTAGGGn

• Published in: Nucleic acids research Vol. 20; no. 24; pp. 6461 - 6464
• Main Authors: McKay, Stewart J., Cooke, Howard
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 25.12.1992
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Antibodies, Monoclonal; Base Sequence; Binding and carrier proteins; Binding Sites; Binding, Competitive; Biological and medical sciences; DNA - metabolism; DNA-Binding Proteins - metabolism; Fundamental and applied biological sciences. Psychology; Heterogeneous-Nuclear Ribonucleoprotein Group A-B; Heterogeneous-Nuclear Ribonucleoproteins; Immunoblotting; Liver - metabolism; Mice; Molecular Sequence Data; Nuclear Proteins - isolation & purification; Nuclear Proteins - metabolism; Oligodeoxyribonucleotides; Plasmids; Proteins; Repetitive Sequences, Nucleic Acid; Ribonucleoproteins - immunology; Ribonucleoproteins - isolation & purification; Ribonucleoproteins - metabolism; RNA - metabolism; RNA-Binding Proteins - metabolism; Vertebrates; Sequence specificity; Vertebrata; Ribonucleoprotein; Mammalia; Mouse; Repeated sequence; Liver; Rodentia; DNA binding protein; Molecular interaction; Telomer
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/20.24.6461

We have previously isolated a protein from mouse liver nuclei that specifically binds to single stranded (TTAGGG)n repeats. TTAGGG is the telomeric repeats of mammals and we therefore named the new protein single stranded telomere binding protein (sTBP). Further studies now identify sTBP as heterogeneous nuclear ribonucleoprotein (hnRNP) A2/B1 on the basis of amino acid sequence determination and antibody reactivity. A2 and B1 form a major part of the protein component of hnRNP particles and are abundant nuclear proteins. Unexpectedly, A2/B1 has a high specificity for binding to the RNA equivalent of TTAGGG, UUAGGG, but under the same conditions does not appear to have a strong affinity for a number of other RNA species.