|Genes and Development (2003) 17(4):461-75|
|Northeast Structural Genomics Consortium|
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The PWI motif is a highly conserved domain of unknown function in the SRm160 splicing and 3'-end cleavage-stimulatory factor, as well as in several other known or putative pre-mRNA processing components. ...
We show here that the PWI motif is a new type of RNA/DNA-binding domain that has an equal preference for single- and double-stranded nucleic acids. Deletion of the motif prevents SRm160 from binding RNA and stimulating 3'-end cleavage, and its substitution with a heterologous RNA-binding domain restores these functions. The NMR solution structure of the SRm160-PWI motif reveals a novel, four-helix bundle and represents the first example of an alpha-helical fold that can bind single-stranded (ss)RNA. Structure-guided mutagenesis indicates that the same surface is involved in RNA and DNA binding and requires the cooperative action of a highly conserved, adjacent basic region. Thus, the PWI motif is a novel type of nucleic acid-binding domain that likely has multiple important functions in pre-mRNA processing, including SRm160-dependent stimulation of 3'-end formation.
|metabolism chemistry genetics |
|Binding Sites Humans Amino Acid Motifs Amino Acid Sequence Conserved Sequence Models, Molecular Molecular Sequence Data Nucleic Acids RNA-Binding Proteins Protein Conformation RNA Splicing RNA Processing, Post-Transcriptional Magnetic Resonance Spectroscopy Sequence Deletion HeLa Cells RNA Precursors Antigens, Nuclear Nuclear Matrix-Associated Proteins |
|34 (Last update: 03/16/2019 5:22:34pm)|
|Genes Dev. 2003 Feb 15;17(4):461-75.|