A multifunctional RNA recognition motif in poly(A)-specific ribonuclease with cap and poly(A) binding properties
Autor
Nilsson, P.; Henriksson, N.; Niedzwiecka, A.; Balatsos, N. A. A.; Kokkoris, K.; Eriksson, J.; Virtanen, A.Fecha
2007Materia
Resumen
Poly(A)-specific ribonuclease (PARN) is an oligomeric, processive and cap-interacting 3′ exoribonuclease that efficiently degrades mRNA poly(A) tails. Here we show that the RNA recognition motif (RRM) of PARN harbors both poly(A) and cap binding properties, suggesting that the RRM plays an important role for the two critical and unique properties that are tightly associated with PARN activity, i.e. recognition and dependence on both the cap structure and poly(A) tail during poly(A) hydrolysis. We show that PARN and its RRM have micromolar affinity to the cap structure by using fluorescence spectroscopy and nanomolar affinity for poly(A) by using filter binding assay. We have identified one tryptophan residue within the RRM that is essential for cap binding but not required for poly(A) binding, suggesting that the cap- and poly(A)-binding sites associated with the RRM are both structurally and functionally separate from each other. RRM is one of the most commonly occurring RNA-binding domains identified so far, suggesting that other RRMs may have both cap and RNA binding properties just as the RRM of PARN. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.
Colecciones
Ítems relacionados
Mostrando ítems relacionados por Título, autor o materia.
-
Investigating Molecular Determinants of Cancer Cell Resistance to Ionizing Radiation Through an Integrative Bioinformatics Approach
Toy H.I., Karakülah G., Kontou P.I., Alotaibi H., Georgakilas A.G., Pavlopoulou A. (2021)Eradication of cancer cells through exposure to high doses of ionizing radiation (IR) is a widely used therapeutic strategy in the clinical setting. However, in many cases, cancer cells can develop remarkable resistance ... -
Enhancer of rudimentary homologue interacts with scaffold attachment factor B at the nuclear matrix to regulate SR protein phosphorylation
Drakouli S., Lyberopoulou A., Papathanassiou M., Mylonis I., Georgatsou E. (2017)Scaffold attachment factor B1 (SAFB1) is an integral component of the nuclear matrix of vertebrate cells. It binds to DNA on scaffold/matrix attachment region elements, as well as to RNA and a multitude of different proteins, ... -
Proteomic analysis of the mitochondrial glucocorticoid receptor interacting proteins reveals pyruvate dehydrogenase and mitochondrial 60 kDa heat shock protein as potent binding partners
Karra A.G., Sioutopoulou A., Gorgogietas V., Samiotaki M., Panayotou G., Psarra A.-M.G. (2022)Glucocorticoids are steroid hormones that regulate plethora biological actions such as growth and metabolism, immune response, and apoptosis. Glucocorticoids actions are mediated via glucocorticoid receptors which act ...