Article
The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
Author/s | Díaz Moreno, Irene
García Mayoral, María Flor Hollingworth, David Ramos, Andrés |
Department | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular |
Publication Date | 2008 |
Deposit Date | 2019-03-26 |
Published in |
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Abstract | K-homology (KH) splicing regulator protein (KSRP) is a multi-domain RNA-binding protein that regulates different steps of mRNA metabolism, from mRNA splicing to mRNA decay, interacting with a broad range of RNA sequences. ... K-homology (KH) splicing regulator protein (KSRP) is a multi-domain RNA-binding protein that regulates different steps of mRNA metabolism, from mRNA splicing to mRNA decay, interacting with a broad range of RNA sequences. To understand how KSRP recognizes its different RNA targets it is necessary to define the general rules of KSRP-RNA interaction. We describe here a complete scaffold-independent analysis of the RNA-binding potential of the four KH domains of KSRP. The analysis shows that KH3 binds to the RNA with a significantly higher affinity than the other domains and recognizes specifically a G-rich target. It also demonstrates that the other KH domains of KSRP display different sequence preferences explaining the broad range of targets recognized by the protein. Further, KSRP shows a strong negative selectivity for sequences containing several adjacent Cytosines limiting the target choice of KSRP within single-stranded RNA regions. The in-depth analysis of the RNA-binding potential of the KH domains of KSRP provides us with an understanding of the role of low sequence specificity domains in RNA recognition by multi-domain RNA-binding proteins. |
Project ID. | WT082088MA
240-2005 |
Citation | Díaz Moreno, I., García Mayoral, M.F., Hollingworth, D. y Ramos, A. (2008). The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets. Nucleic Acids Research, 36 (16), 5290-5296. |
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