Journal
MOLECULAR CELL
Volume 7, Issue 1, Pages 227-232Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(01)00170-8
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM062264, R29GM048752] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM062264, R29 GM48752] Funding Source: Medline
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While some members of the ubiquitous DExD/H box family of proteins have RNA helicase activity in vitro, their roles in vivo remain virtually unknown. Here, we show that the function of an otherwise essential DEAD box protein, Prp28p, can be bypassed by mutations that alter either the protein U1-C or the U1 small nuclear RNA. Further analysis suggests that the conserved L13 residue in the U1-C protein makes specific contact to stabilize the U1 snRNA/5' splice site duplex in the prespliceosome, and that Prp28p functions to counteract the stabilizing effect of the U1-C protein, thereby promoting the dissociation of the U1 small nuclear ribonucleoprotein particle from the 5' splice site. Thus, in addition to unwinding RNA, the DExD/H box proteins may affect RNA-RNA rearrangements by antagonizing specific RNA-stabilizing proteins.
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