Histone H3 N-terminal peptide binds directly to its own mRNA: a possible mode of feedback inhibition to control translation

Title
Histone H3 N-terminal peptide binds directly to its own mRNA: a possible mode of feedback inhibition to control translation
Authors
이경현이남주현순실박용근양은경이준규정선주유재훈
Keywords
aptamers; feedback inhibition; histone H3; RNA; SELEX
Issue Date
2009-05
Publisher
Chembiochem : a European journal of chemical biology
Citation
VOL 10, NO 8, 1313-1316
Abstract
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 cells.
URI
http://pubs.kist.re.kr/handle/201004/45532
ISSN
1439-4227
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KIST Publication > Article
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