Nucleic Acids Research, Vol 24, Issue 12 2441-2449, Copyright © 1996 by Oxford University Press
MA Hess and RF Duncan
Preferential translation of Drosophila heat shock protein 70 (Hsp70) mRNA
requires only the 5'-untranslated region (5'-UTR). The sequence of this
region suggests that it has relatively little secondary structure, which
may facilitate efficient protein synthesis initiation. To determine whether
minimal 5'-UTR secondary structure is required for preferential translation
during heat shock, the effect of introducing stem-loops into the Hsp70 mRNA
5'-UTR was measured. Stem-loops of -11 kcal/mol abolished translation
during heat shock, but did not reduce translation in non-heat shocked
cells. A -22 kcal/mol stem-loop was required to comparably inhibit
translation during growth at normal temperatures. To investigate whether
specific sequence elements are also required for efficient preferential
translation, deletion and mutation analyses were conducted in a truncated
Hsp70 5'-UTR containing only the cap-proximal and AUG-proximal segments.
Linker-scanner mutations in the cap-proximal segment (+1 to +37) did not
impair translation. Re-ordering the segments reduced mRNA translational
efficiency by 50%. Deleting the AUG-proximal segment severely inhibited
translation. A 5-extension of the full-length leader specifically impaired
heat shock translation. These results indicate that heat shock reduces the
capacity to unwind 5-UTR secondary structure, allowing only mRNAs with
minimal 5'-UTR secondary structure to be efficiently translated. A function
for specific sequences is also suggested.
ARTICLES
Sequence and structure determinants of Drosophila Hsp70 mRNA translation: 5'UTR secondary structure specifically inhibits heat shock protein mRNA translation
Department of Molecular Pharmacology and Toxicology, University of Southern California School of Pharmacy, Los Angeles, CA 90033, USA.
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