Nucleic Acids Research, Vol 25, Issue 24 5033-5040, Copyright © 1997 by Oxford University Press
TH Chang, LJ Latus, Z Liu and JM Abbott
The yeast PRP28 g ene has been implicated in nuclear precursor messenger
RNA (pre-mRNA) splicing, a two-step reaction involved in a multitude of RNA
structural alterations. Prp28p, the gene product of PRP28 , is a member of
the evolutionarily conserved DEAD-box proteins (DBPs). Members of DBPs are
involved in a variety of RNA-related biochemical processes, presumably by
their putative RNA helicase activities. Prp28p has been speculated to play
a role in melting the duplex between U4 and U6 small nuclear RNAs (snRNAs),
leading to the formation of an active spliceosome. To study the function of
Prp28p and its interactions with other components of the splicing
machinery, we have isolated and characterized a large number of prp28
conditional mutants. Strikingly, many of these prp28 mutations are
localized in the highly conserved motifs found in all the DBPs. Intragenic
reversion analysis suggests that regions of motifs II, III and V, as well
as of motifs I and IV, in Prp28p are likely to be in close proximity to
each other. Our results thus provide the first hint of the local structural
arrangement for Prp28p, and perhaps for other DBPs as well.
ARTICLES
Genetic interactions of conserved regions in the DEAD-box protein Prp28p
Department of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA. chang.108@osu.edu
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