title: The global regulator RNase III modulates translation repression by the transcription elongation factor N.
abstract: Efficient expression of most bacteriophage lambda early genes depends upon the formation of an antiterminating transcription complex to overcome transcription terminators in the early operons, p(L) and p(R). Formation of this complex requires the phage-encoded protein N, the first gene product expressed from the p(L) operon. The N leader RNA contains, in this order: the NUTL site, an RNase III-sensitive hairpin and the N ribosome-binding site. N bound to NUTL RNA is part of both the antitermination complex and an autoregulatory complex that represses the translation of the N gene. In this study, we show that cleavage of the N leader by RNase III does not inhibit antitermination but prevents N-mediated translation repression of N gene expression. In fact, by preventing N autoregulation, RNase III activates N gene translation at least 200-fold. N-mediated translation repression is extremely sensitive to growth rate, reflecting the growth rate regulation of RNase III expression itself. Given N protein's critical role in lambda development, the level of RNase III activity therefore serves as an important sensor of physiological conditions for the bacteriophage.
authors.affiliation: Molecular Control and Genetics Section, Gene Regulation and Chromosome Biology, National Cancer Institute-Frederick, National Institutes of Health, Frederick, MD 21702-1201, USA.
authors.forename: Helen R
authors.initials: HR
authors.lastname: Wilson
authors.forename: Daiguan
authors.initials: D
authors.lastname: Yu
authors.forename: Howard K
authors.initials: HK
authors.lastname: Peters
authors.forename: Jian-guang
authors.initials: JG
authors.lastname: Zhou
authors.forename: Donald L
authors.initials: DL
authors.lastname: Court
mesh_terms: D020121:5' Untranslated Regions / Q000378:metabolism; D010582:Bacteriophage lambda / Q000502:physiology; D001483:Base Sequence; D003470:Culture Media; D004722:Endoribonucleases / Q000502:physiology*; D004926:Escherichia coli / Q000821:virology; D029968:Escherichia coli Proteins / Q000502:physiology*; D005686:Galactokinase / Q000235:genetics; D015967:Gene Expression Regulation, Viral / Q000502:physiology*; D017930:Genes, Reporter; D007763:Lac Operon; D008242:Lysogeny / Q000502:physiology; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D014176:Protein Biosynthesis / Q000502:physiology*; D012322:RNA Precursors / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics; D012097:Repressor Proteins / Q000502:physiology*; D043244:Ribonuclease III; D054334:Viral Regulatory and Accessory Proteins / Q000502:physiology*
chemical_list: D020121:5' Untranslated Regions; D003470:Culture Media; D029968:Escherichia coli Proteins; D046911:Macromolecular Substances; C059417:N protein, Bacteriophage lambda; D012322:RNA Precursors; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins; D054334:Viral Regulatory and Accessory Proteins; D005686:Galactokinase; D004722:Endoribonucleases; D043244:Ribonuclease III; C468366:ribonuclease III, E coli