Structure and RNA binding of the mouse Pumilio-2 Puf domain.
H.T.Jenkins,
R.Baker-Wilding,
T.A.Edwards.
ABSTRACT
Puf proteins control translation through the interaction of a C-terminal Puf
domain with specific sequences present in the 3' untranslated region of
messenger RNAs. In Drosophila, binding of the protein Pumilio to mRNA leads to
translational repression which is required for anterior/posterior patterning
during embryogenesis. The vertebrate Pumilio homologue 2 (Pum2) has been
implicated in controlling germ cell development through interactions with the
RNA binding proteins deleted in azoospermia (DAZ), DAZ-like (DAZL) and BOULE. We
present the 1.6A resolution X-ray crystal structure of the Puf domain from
murine Pum2 and demonstrate that this domain is capable of binding with
nanomolar affinity to RNA sequences from the hunchback Nanos response element
(NRE) and a previously identified Pum2 binding element (PBE).
Literature references that cite this PDB file's key reference
G.Lu,
and
T.M.Hall
(2011).
Alternate modes of cognate RNA recognition by human PUMILIO proteins.
Structure, 19,
361-367.
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.