title: Histone H3 N-terminal peptide binds directly to its own mRNA: a possible mode of feedback inhibition to control translation.
abstract: Give me some feedback: In vitro selection of aptamers against the H3 peptide provided specific hairpin RNAs that possess high homology with histone H3 mRNA. The identified H3 hairpin RNA binds specifically to the H3 peptide with micromolar affinity and dose-dependently inhibits in vitro translation of the H3 protein. Consequently, the hairpin RNA and H3 peptide are one of the rare cis- and trans-elements on coding regions found among housekeeping proteins in higher eukaryotes.
authors.affiliation: Department of Chemistry and Biology Education, Seoul National University, Seoul 151-742, Korea.
authors.forename: Kyung Hyun
authors.initials: KH
authors.lastname: Lee
authors.forename: Nam Ju
authors.initials: NJ
authors.lastname: Lee
authors.forename: Soonsil
authors.initials: S
authors.lastname: Hyun
authors.forename: Yong Keun
authors.initials: YK
authors.lastname: Park
authors.forename: Eun Gyeong
authors.initials: EG
authors.lastname: Yang
authors.forename: Jun-Kyu
authors.initials: JK
authors.lastname: Lee
authors.forename: Sunjoo
authors.initials: S
authors.lastname: Jeong
authors.forename: Jaehoon
authors.initials: J
authors.lastname: Yu
mesh_terms: D052157:Aptamers, Nucleotide / Q000378:metabolism; D001483:Base Sequence; D025461:Feedback, Physiological; D006657:Histones / Q000235:genetics* / Q000378:metabolism; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology*; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000737:chemistry* / Q000378:metabolism
chemical_list: D052157:Aptamers, Nucleotide; D006657:Histones; D010455:Peptides; D012333:RNA, Messenger