Histone H3 N-terminal peptide binds directly to its own mRNA: a possible mode of feedback inhibition to control translation
- Histone H3 N-terminal peptide binds directly to its own mRNA: a possible mode of feedback inhibition to control translation
- 이경현; 이남주; 현순실; 박용근; 양은경; 이준규; 정선주; 유재훈
- aptamers; feedback inhibition; histone H3; RNA; SELEX
- Issue Date
- Chembiochem : a European journal of chemical biology
- VOL 10, NO 8, 1313-1316
- In summary, by using the SELEX method against the H3 peptide
we have identified a 31-nt hairpin RNA that is located in
the coding region of H3 mRNA and serves as a cis-element.
The short hairpin RNA, which is transcribed in vitro,
has micromolar affinity against H3 peptide. In vitro
translation of the H3 protein was inhibited by the H3
peptide in a dose-dependent manner. Furthermore,
addition of H3 hairpin RNA restored H3 protein expression.
The expression level of transfected luciferase
was reduced to around 60% with the H3 hairpin,
while no reductions were observed with inserted RRE
hairpin and other controls in a 293A cell-based assay.
Thus, the pair comprised of hairpin RNA in the H3
coding region and the cognate peptide is one of the
rare cis-elements on coding regions found in higher
eukaryotes. A possibility exists that more hairpin
RNAs are inhibited by their products and, as such,
this might serve as general feedback regulation. This
regulatory mechanism might be required for the control
of highly abundant housekeeping proteins in
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