title: The role of the OOP antisense RNA in coliphage lambda development.
abstract: We have made a derivative of bacteriophage lambda that makes no OOP antisense RNA. The mutant phage carries a point mutation that inactivates the OOP promoter, po. The phages lambda + and lambda po- have identical plaque morphologies, one-step growth curves, and frequencies of lysogenization of a sensitive host. OOP RNA synthesis is weakly repressed by the Escherichia coli LexA protein. Consonant with this inducibility of OOP RNA synthesis by ultraviolet light, we find a two-fold greater phage burst following ultraviolet induction of a lambda + than of a lambda po- prophage. In lambda + infections, OOP RNA causes two cleavage events in cll mRNA: one is in the 3'-end of the coding region, and the second is in the intercistronic region between the cll and O genes. The cll gene fragments are subject to additional hydrolytic events, and cll mRNA levels are several-fold lower in lambda + than in lambda po- infections late in the infection cycle. However, O mRNA levels are almost unaffected by the po- mutation.
authors.affiliation: Department of Biological Sciences, State University of New York, Albany 12222.
authors.forename: L
authors.initials: L
authors.lastname: Krinke
authors.forename: M
authors.initials: M
authors.lastname: Mahoney
authors.forename: D L
authors.initials: DL
authors.lastname: Wulff
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D010582:Bacteriophage lambda / Q000235:genetics* / Q000254:growth & development; D001483:Base Sequence; D004722:Endoribonucleases / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins; D015967:Gene Expression Regulation, Viral / Q000528:radiation effects; D005814:Genes, Viral; D008242:Lysogeny; D008969:Molecular Sequence Data; D011401:Promoter Regions, Genetic; D012323:RNA Processing, Post-Transcriptional; D016372:RNA, Antisense / Q000502:physiology*; D012333:RNA, Messenger / Q000378:metabolism; D012367:RNA, Viral / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012097:Repressor Proteins / Q000378:metabolism; D043244:Ribonuclease III; D012697:Serine Endopeptidases; D014157:Transcription Factors / Q000096:biosynthesis / Q000235:genetics*; D014466:Ultraviolet Rays; D014764:Viral Proteins; D015678:Viral Structural Proteins / Q000235:genetics*; D014775:Virus Activation; D000099160:LexA Repressor Protein
chemical_list: D001426:Bacterial Proteins; D004722:Endoribonucleases; D029968:Escherichia coli Proteins; D016372:RNA, Antisense; D012333:RNA, Messenger; D012367:RNA, Viral; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins; D043244:Ribonuclease III; D012697:Serine Endopeptidases; D014157:Transcription Factors; D014764:Viral Proteins; D015678:Viral Structural Proteins; D000099160:LexA Repressor Protein; C039000:cII protein, bacteriophage lambda; C468366:ribonuclease III, E coli