PMID- 10535969
OWN - NLM
STAT- MEDLINE
DCOM- 19991210
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 22
DP  - 1999 Oct 26
TI  - The STAR protein QKI-6 is a translational repressor.
PG  - 12605-10
AB  - The signal transduction and activation of RNA (STAR) family of RNA-binding
      proteins, whose members are evolutionarily conserved from yeast to humans, are
      important for a number of developmental decisions. For example, in the mouse,
      quaking proteins (QKI-5, QKI-6, and QKI-7) are essential for embryogenesis and
      myelination, whereas a closely related protein in Caenorhabditis elegans,
      germline defective-1 (GLD-1), is necessary for germ-line development. Recently,
      GLD-1 was found to be a translational repressor that acts through regulatory
      elements, called TGEs (for tra-2 and GLI elements), present in the 3'
      untranslated region of the sex-determining gene tra-2. This gene promotes female 
      development, and repression of tra-2 translation by TGEs is necessary for the
      male cell fates. The finding that GLD-1 inhibits tra-2 translation raises the
      possibility that other STAR family members act by a similar mechanism to control 
      gene activity. Here we demonstrate, both in vitro and in vivo, that QKI-6
      functions in the same manner as GLD-1 and can specifically bind to TGEs to
      repress translation of reporter constructs containing TGEs. In addition,
      expression of QKI-6 in C. elegans wild-type hermaphrodites or in hermaphrodites
      that are partially masculinized by a loss-of-function mutation in the
      sex-determining gene tra-3 results in masculinization of somatic tissues,
      consistent with QKI-6 repressing the activity of tra-2. These results strongly
      suggest that QKI-6 may control gene activity by operating through TGEs to
      regulate translation. In addition, our data support the hypothesis that other
      STAR family members may also be TGE-dependent translational regulators.
FAU - Saccomanno, L
AU  - Saccomanno L
AD  - Department of Cell Biology, Northwestern University Medical School, Chicago, IL
      60611, USA.
FAU - Loushin, C
AU  - Loushin C
FAU - Jan, E
AU  - Jan E
FAU - Punkay, E
AU  - Punkay E
FAU - Artzt, K
AU  - Artzt K
FAU - Goodwin, E B
AU  - Goodwin EB
LA  - eng
GR  - GM 5186-01/GM/NIGMS NIH HHS/United States
GR  - R01 GM051836/GM/NIGMS NIH HHS/United States
GR  - HD 30658/HD/NICHD NIH HHS/United States
GR  - R01 HD010668/HD/NICHD NIH HHS/United States
GR  - HD 10668/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (3' Untranslated Regions)
RN  - 0 (DNA Primers)
RN  - 0 (RNA-Binding Proteins)
SB  - IM
MH  - 3' Untranslated Regions
MH  - Animals
MH  - Animals, Genetically Modified
MH  - Base Sequence
MH  - Caenorhabditis elegans/cytology/metabolism
MH  - DNA Primers
MH  - Female
MH  - Male
MH  - Mice
MH  - Protein Biosynthesis/*physiology
MH  - RNA-Binding Proteins/genetics/*physiology
MH  - Signal Transduction/*physiology
PMC - PMC23011
EDAT- 1999/10/27 00:00
MHDA- 1999/10/27 00:01
CRDT- 1999/10/27 00:00
PHST- 1999/10/27 00:00 [pubmed]
PHST- 1999/10/27 00:01 [medline]
PHST- 1999/10/27 00:00 [entrez]
AID - 10.1073/pnas.96.22.12605 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12605-10. doi:
      10.1073/pnas.96.22.12605.