Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA

Article Abstract:

The crystal structure of the two-RNA-recognition motif (two-RRM) domain of hnRNP A1 (UP1), or unwinding protein, the amino-terminal domain of human hnRNP A1, has been determined at resolution of 2.1 angstrom. The structure of the complex shows structure responsible for sequence-specific recognition by hnRNP A1 of the single-stranded overhangs of human telomeres. Human hnRNP is a versatile nucleic acid-binding protein with one strand. It acts in some parts of mRNA maturation and in length regulation for telomeres. Models for juxtaposition of other possible 5' splice sites and for regular packaging of telomere 3' overhangs are suggested.

Analysis, Usage, Telomeres, RNA, Chromosome mapping, Crystals, Crystal structure, Genetic disorders, X-ray crystallography, Heredity, Human, Human heredity

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Allele-specific genetic interactions between Prp8 and RNA active site residues suggest a function for Prp8 at the catalytic core of the spliceosome

Article Abstract:

Interactions between Prp8 and RNA active site residues are discussed relative to a genetic approach taken in Saccharomyces cerevisiae to find functional correlates to Prp8 cross-linking interactions with RNA. These allele-specific genetic interactions suggest a function for Prp8 at the spliceosome catalytic core and it is proposed that Prp8 takes part in a till-now unrecognized tertiary interaction between U6 smRNA and the 5' and 3' ends of the intron.

Statistical Data Included, Genetic aspects, Physiological regulation, Saccharomyces, Biological control systems, RNA splicing, Messenger RNA, Allelomorphism, Alleles

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