Nucleic Acids Research, Vol 24, Issue 19 3739-3747, Copyright © 1996 by Oxford University Press
GM Lamm, SM Nicol, FV Fuller-Pace and AI Lamond
P72, a novel human member of the DEAD box family of putative RNA- dependent
ATPases and ATP-dependent RNA helicases was isolated from a HeLa cDNA
library. The predicted amino acid sequence of p72 is highly homologous to
that of the prototypic DEAD box protein p68. In addition to the conserved
core domains characteristic of DEAD box proteins, p72 contains several
N-terminal RGG RNA-binding domains and a serine/glycine rich C-terminus
likely involved in mediating protein- protein interactions. 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 p72 exhibits ATPase
activity in the presence of a range of RNA moieties. Immunocytochemical
studies of p68 and p72 show that these proteins localise to similar
locations in the nucleus of HeLa cells, suggesting their involvement in a
nuclear process.
ARTICLES
p72: a human nuclear DEAD box protein highly related to p68
Research Institute of Molecular Pathology, Vienna, Austria.
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