ATP-Dependent roX RNA Remodeling by the Helicase maleless Enables Specific Association of MSL Proteins
RNA Helicase A
DOI:
10.1016/j.molcel.2013.06.011
Publication Date:
2013-07-20T14:45:39Z
AUTHORS (5)
ABSTRACT
Highlights•MLE binds with preference to a conserved stem-loop structure in roX RNA•ATP-dependent unwinding of the stem creates an alternative MLE-roX structure•RNA remodeling is prerequisite for selective MSL2 interaction•Remodeling may constitute switch initiate assembly MSL-DCCSummaryDosage compensation Drosophila involves global activation genes on male X chromosome. The activating complex (MSL-DCC) consists male-specific-lethal (MSL) proteins and two long, noncoding RNAs. RNAs are essential X-chromosomal targeting, but their contributions MSL-DCC function enigmatic. Conceivably, RNA helicase MLE, itself MSL subunit, actively involved incorporating into functional DCC. We determined secondary roX2 mapped specific interaction sites MLE vitro. Upon addition ATP, disrupted functionally important loop roX2. This enhanced ATP-dependent association MSL2, core subunit MSL-DCC, providing link between subunits. Probing conformation vivo revealed remodeled chromatin-bound active stable by rate-limiting step assembly.
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