title: RNA-binding properties and RNA chaperone activity of human peroxiredoxin 1.
abstract: Human peroxiredoxin 1 (hPrx1), a member of the peroxiredoxin family, detoxifies peroxide substrates and has been implicated in numerous biological processes, including cell growth, proliferation, differentiation, apoptosis, and redox signaling. To date, Prx1 has not been implicated in RNA metabolism. Here, we investigated the ability of hPrx1 to bind RNA and act as an RNA chaperone. In vitro, hPrx1 bound to RNA and DNA, and unwound nucleic acid duplexes. hPrx1 also acted as a transcription anti-terminator in an assay using an Escherichia coli strain containing a stem-loop structure upstream of the chloramphenicol resistance gene. The overall cellular level of hPrx1 expression was not increased at low temperatures, but the nuclear level of hPrx1 was increased. In addition, hPrx1 overexpression enhanced the survival of cells exposed to cold stress, whereas hPrx1 knockdown significantly reduced cell survival under the same conditions. These findings suggest that hPrx1 may perform biological functions as a RNA-binding protein, which are distinctive from known functions of hPrx1 as a reactive oxygen species scavenger.
authors.affiliation: Lee Gil Ya Cancer and Diabetes Institute, Gachon University, Republic of Korea.
authors.forename: Ji-Hee
authors.initials: JH
authors.lastname: Kim
authors.forename: Jeong-Mi
authors.initials: JM
authors.lastname: Lee
authors.forename: Hae Na
authors.initials: HN
authors.lastname: Lee
authors.forename: Eun-Kyung
authors.initials: EK
authors.lastname: Kim
authors.forename: Bin
authors.initials: B
authors.lastname: Ha
authors.forename: Sung-Min
authors.initials: SM
authors.lastname: Ahn
authors.forename: Ho Hee
authors.initials: HH
authors.lastname: Jang
authors.forename: Sang Yeol
authors.initials: SY
authors.lastname: Lee
mesh_terms: D002467:Cell Nucleus / Q000378:metabolism; D002470:Cell Survival; D002701:Chloramphenicol / Q000494:pharmacology; D057773:Cold Shock Proteins and Peptides; D058639:Cold-Shock Response; D024881:Drug Resistance, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics; D029968:Escherichia coli Proteins / Q000235:genetics; D006367:HeLa Cells; D006360:Heat-Shock Proteins / Q000235:genetics; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D009690:Nucleic Acid Conformation; D054464:Peroxiredoxins / Q000378:metabolism*; D012313:RNA / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D017382:Reactive Oxygen Species / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*; D014158:Transcription, Genetic
chemical_list: D057773:Cold Shock Proteins and Peptides; C498192:CspA protein, E coli; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D016601:RNA-Binding Proteins; D017382:Reactive Oxygen Species; D014157:Transcription Factors; D012313:RNA; D002701:Chloramphenicol; C515940:PRDX1 protein, human; D054464:Peroxiredoxins