title: RNase E enzymes from rhodobacter capsulatus and Escherichia coli differ in context- and sequence-dependent in vivo cleavage within the polycistronic puf mRNA.
abstract: The 5' pufQ mRNA segment and the pufLMX mRNA segment of Rhodobacter capsulatus exhibit different stabilities. Degradation of both mRNA segments is initiated by RNase E-mediated endonucleolytic cleavage. While Rhodobacter RNase E does not discriminate between the different sequences present around the cleavage sites within pufQ and pufL, Escherichia coli RNase E shows preference for the sequence harboring more A and U residues.
authors.affiliation: Institut für Mikrobiologie und Molekularbiologie, D-35392 Giessen, Germany.
authors.forename: C
authors.initials: C
authors.lastname: Heck
authors.forename: E
authors.initials: E
authors.lastname: Evguenieva-Hackenberg
authors.forename: A
authors.initials: A
authors.lastname: Balzer
authors.forename: G
authors.initials: G
authors.lastname: Klug
mesh_terms: D001426:Bacterial Proteins; D004722:Endoribonucleases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D045342:Light-Harvesting Protein Complexes; D009690:Nucleic Acid Conformation; D045322:Photosynthetic Reaction Center Complex Proteins / Q000235:genetics / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism*; D016354:Rhodobacter capsulatus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; C096433:PufL protein, Bacteria; D012333:RNA, Messenger; D004722:Endoribonucleases; C022537:ribonuclease E