P72, a novel human member of the DEAD box family of putative RNA-depen
dent ATPases and ATP-dependent RNA helicases was isolated from a HeLa
cDNA library, The predicted amino acid sequence of p72 is highly homol
ogous to that of the prototypic DEAD box protein p68, In addition to t
he conserved core domains characteristic of DEAD box proteins, p72 con
tains several N-terminal RGG RNA-binding domains and a serine/glycine
rich C-terminus likely involved in mediating protein-protein interacti
ons. A p72-specific probe detects two mRNAs of approximately 5300 and
9300 bases which, although ubiquitously expressed, show variability in
their expression levels in different tissues, Purified recombinant p7
2 exhibits ATPase activity in the presence of a range of RNA moieties,
Immunocytochemical studies of p68 and p72 show that these proteins lo
calise to similar locations in the nucleus of HeLa cells, suggesting t
heir involvement in a nuclear process.