Locked tether formation by cooperative folding of Rna14p monkeytail and Rna15p hinge domains in the yeast CF IA complex.

doi:10.1016/j.str.2011.02.003

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Article

Locked tether formation by cooperative folding of Rna14p monkeytail and Rna15p hinge domains in the yeast CF IA complex.

Structure (London, England : 1993) - 13 Apr 2011

Moreno-Morcillo Maria, Minvielle-Sébastia Lionel, Fribourg Sébastien, Mackereth Cameron D

Abstract excerpt

The removal of the 3' region of pre-mRNA followed by polyadenylation is a key step in mRNA maturation. In the yeast Saccharomyces cerevisiae, one component of the processing machinery is the cleavage/polyadenylation factor IA (CF IA) complex, composed of four proteins (Clp1p, Pcf11p, Rna14p, Rna15p) that recognize RNA sequences adjacent to the cleavage site and recruit additional processing factors. To gain...

Topics

Amino Acid Sequence
Binding Sites
Circular Dichroism
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Mutation
Protein Binding
Protein Folding
Protein Multimerization
Protein Structure, Tertiary
Protein Unfolding
Saccharomyces cerevisiae

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Open in PubMed

Identifiers

PMID: 21481776
DOI: 10.1016/j.str.2011.02.003

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Saccharomyces cerevisiae Proteins

Sequence Homology, Amino Acid

Solutions

mRNA Cleavage and Polyadenylation Factors