title: RNA methylation under heat shock control.
abstract: Structural, biochemical, and genetic techniques were applied to investigate the function of FtsJ, a recently identified heat shock protein. FtsJ is well conserved, from bacteria to humans. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. The molecular surface of FtsJ exposes a putative nucleic acid binding groove composed of highly conserved, positively charged residues. Substrate analysis showed that FtsJ methylates 23S rRNA within 50S ribosomal subunits in vitro and in vivo. Null mutations in ftsJ show a dramatically altered ribosome profile, a severe growth disadvantage, and a temperature-sensitive phenotype. Our results reveal an unexpected link between the heat shock response and RNA metabolism.
authors.affiliation: Department of Biology, University of Michigan, Ann Arbor 48109, USA.
authors.forename: H
authors.initials: H
authors.lastname: Bügl
authors.forename: E B
authors.initials: EB
authors.lastname: Fauman
authors.forename: B L
authors.initials: BL
authors.lastname: Staker
authors.forename: F
authors.initials: F
authors.lastname: Zheng
authors.forename: S R
authors.initials: SR
authors.lastname: Kushner
authors.forename: M A
authors.initials: MA
authors.lastname: Saper
authors.forename: J C
authors.initials: JC
authors.lastname: Bardwell
authors.forename: U
authors.initials: U
authors.lastname: Jakob
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017360:Arabidopsis / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D017173:Caenorhabditis elegans / Q000235:genetics; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D017017:Methanococcus / Q000235:genetics; D008745:Methylation; D008780:Methyltransferases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D017433:Protein Structure, Secondary; D012338:RNA, Ribosomal, 23S / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism; D012436:S-Adenosylmethionine / Q000378:metabolism; D012568:Schizosaccharomyces / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D012338:RNA, Ribosomal, 23S; D011994:Recombinant Proteins; D012436:S-Adenosylmethionine; D008780:Methyltransferases