hnRNP A2/B1 binds specifically to single stranded vertebrate telomeric repeat TTAGGGn
- 25 December 1992
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 20 (24) , 6461-6464
- https://doi.org/10.1093/nar/20.24.6461
Abstract
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.Keywords
This publication has 16 references indexed in Scilit:
- A protein which specifically binds to single stranded TTAGGGnrepeatsNucleic Acids Research, 1992
- Renaturation of complementary DNA strands mediated by purified mammalian heterogeneous nuclear ribonucleoprotein A1 protein: implications for a mechanism for rapid molecular assembly.Proceedings of the National Academy of Sciences, 1990
- Conservation of the human telomere sequence (TTAGGG)n among vertebrates.Proceedings of the National Academy of Sciences, 1989
- Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formationTrends in Biochemical Sciences, 1988
- Modulation of hnRNP A1 protein gene expression by epidermal growth factor in Rat-1 cellsNucleic Acids Research, 1988
- The core proteins of 35 S hnRNP complexesEuropean Journal of Biochemistry, 1985
- Chromatin structure of the molecular ends of oxytricha macronuclear DNA: phased nucleosomes and a telomeric complexCell, 1984
- Higher order DNA structure in macronuclear chromatin of the hypotrichous ciliate Oxytricha nova.Proceedings of the National Academy of Sciences, 1982
- All gene-sized DNA molecules in four species of hypotrichs have the same terminal sequence and an unusual 3' terminus.Proceedings of the National Academy of Sciences, 1981
- Identification and characterization of the packaging proteins of core 40S hnRNP particlesCell, 1977