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

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 heteroge...

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Veröffentlicht in:	Nucleic acids research 1992-12, Vol.20 (24), p.6461-6464
Hauptverfasser:	McKay, Stewart J., Cooke, Howard
Format:	Artikel
Sprache:	eng
Schlagworte:	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
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Zusammenfassung:	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.
ISSN:	0305-1048 1362-4962
DOI:	10.1093/nar/20.24.6461