Garrey SM, et al. (2006) An extended RNA binding site for the yeast branch point-binding protein and the role of its zinc knuckle domains in RNA binding. J Biol Chem 281(37):27443-53
Abstract: The highly conserved branchpoint sequence (BPS) of UACUAAC in Saccharomyces cerevisiae is initially recognized by the branchpoint binding protein (BBP). Using systematic evolution of ligands by exponential enrichment (SELEX) we have determined that yeast BBP binds the branchpoint sequence UACUAAC with highest affinity and prefers an additional adenosine downstream of the BPS. Furthermore, we also found that a stem-loop upstream of the BPS enhances binding, both to an artificially designed RNA (30-fold effect) and to an RNA from a yeast intron (3-fold effect). The Zn knuckles of BBP are partially responsible for the enhanced binding to the stem-loop but do not appear to have a significant role in the binding of BBP to single-strand RNA substrates. C-terminal deletions of BBP reveal that the linker regions between the two Zn knuckles and between the N-terminal RNA binding domains (KH and QUA2 domains) and the first Zn knuckle, are important for binding to RNA. The lack of involvement of the second highly conserved Zn knuckle in RNA binding suggests that this Zn knuckle plays a different role in RNA processing than enhancing the binding of BBP to the BPS.
|Status: Published||Type: Journal Article||PubMed ID: 16861232|
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