Sequence-Specific RNA Binding by a Nova KH Domain
نویسندگان
چکیده
منابع مشابه
Sequence-Specific RNA Binding by a Nova KH Domain Implications for Paraneoplastic Disease and the Fragile X Syndrome
The structure of a Nova protein K homology (KH) domain recognizing single-stranded RNA has been determined at 2.4 A resolution. Mammalian Nova antigens (1 and 2) constitute an important family of regulators of RNA metabolism in neurons, first identified using sera from cancer patients with the autoimmune disorder paraneoplastic opsoclonus-myoclonus ataxia (POMA). The structure of the third KH d...
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The KH domain is an evolutionarily conserved sequence motif present in many RNA-binding proteins, including the pre-mRNA-binding (hnRNP) K protein and the fragile X mental retardation gene product (FMR1). We assessed the role of KH domains in RNA binding by mutagenesis of KH domains in hnRNP K and FMR1. Conserved residues of all three hnRNP K KH domains are required for its wild-type RNA bindin...
متن کاملRegulation of RNA-binding by KH domains of CRD-BP
The ability of its four heterogeneous nuclear ribonucleoprotein-K-homology (KH) domains to physically associate with oncogenic mRNAs is a major criterion for the function of Coding Region Determinant-Binding Protein (CRD-BP). However, the particular RNA binding role of each of the KH domains remains largely unresolved. Here, we mutated the first glycine to an aspartate in the universally conser...
متن کاملStructure and RNA binding of the third KH domain of poly(C)-binding protein 1
Poly(C)-binding proteins (CPs) are important regulators of mRNA stability and translational regulation. They recognize C-rich RNA through their triple KH (hn RNP K homology) domain structures and are thought to carry out their function though direct protection of mRNA sites as well as through interactions with other RNA-binding proteins. We report the crystallographically derived structure of t...
متن کاملSequence-specific RNA binding mediated by the RNase PH domain of components of the exosome.
We have previously demonstrated that PM-Scl-75, a component of the human exosome complex involved in RNA maturation and mRNA decay, can specifically interact with RNAs containing an AU-rich instability element. Through the analysis of a series of deletion mutants, we have now shown that a 266 amino acid fragment representing the RNase PH domain is responsible for the sequence-specific binding t...
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ژورنال
عنوان ژورنال: Cell
سال: 2000
ISSN: 0092-8674
DOI: 10.1016/s0092-8674(00)80668-6