Long-range allostery mediates cooperative adenine nucleotide binding by the Ski2-like RNA helicase Brr2.

ABSTRACT: Brr2 is an essential Ski2-like RNA helicase that exhibits a unique structure among the spliceosomal helicases. Brr2 harbors a catalytically active N-terminal helicase cassette and a structurally similar but enzymatically inactive C-terminal helicase cassette connected by a linker region. Both cassettes contain a nucleotide-binding pocket, but it is unclear whether nucleotide binding in these two pockets is related. Here we use biophysical and computational methods to delineate the functional connectivity between the cassettes and determine whether occupancy of one nucleotide-binding site may influence nucleotide binding at the other cassette. Our results show that Brr2 exhibits high specificity for adenine nucleotides, with both cassettes binding ADP tighter than ATP. Adenine nucleotide af

SUBMITTER: Absmeier E 

PROVIDER: S-EPMC8220420 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature