Home LiteratureArticle Details
PMID: 9303536 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Translational repression by a transcriptional elongation factor.

Genes & development ·Vol. 11 ·No. 17 ·1997-09-01 ·Pages 2204-13

Wilson HR, Kameyama L, Zhou JG, Guarneros G, Court DL

Abstract

One of the classical positive regulators of gene expression is bacteriophage lambda N protein. N regulates the transcription of early phage genes by participating in the formation of a highly processive, terminator-resistant transcription complex and thereby stimulates the expression of genes lying downstream of transcriptional terminators. Also included in this antiterminating transcription complex are an RNA site (NUT) and host proteins (Nus). Here we demonstrate that N has an additional, hitherto unknown regulatory role, as a repressor of the translation of its own gene. N-dependent repression does not occur when NUT is deleted, demonstrating that N-mediated antitermination and translational repression both require the same cis-acting site in the RNA. In addition, we have identified one nut and several host mutations that eliminate antitermination and not translational repression, suggesting the independence of these two N-mediated mechanisms. Finally, the position of nutL with respect to the gene whose expression is repressed is important.

MeSH Terms
Bacteriophage lambda/drug effects,genetics,metabolism Base Sequence Chromosome Mapping DNA Primers/genetics Gene Expression Regulation, Viral Genes, Reporter Genes, Viral Models, Genetic Molecular Sequence Data Mutation Nucleic Acid Conformation Polymerase Chain Reaction Protein Biosynthesis/drug effects RNA, Viral/chemistry,genetics Transcription Factors/genetics,metabolism,pharmacology Viral Regulatory and Accessory Proteins/genetics,metabolism,pharmacology
Chemicals
DNA Primers N protein, Bacteriophage lambda RNA, Viral Transcription Factors Viral Regulatory and Accessory Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Wilson H R
ABL-Basic Research Program, National Cancer Institute-Frederick Cancer Research and Development Center, Maryland 21702-1201, USA.
Kameyama L
Zhou J G
Guarneros G
Court D L
References (71)
71 references, click to expand
  1. Coliphage lambdanutL-: a unique class of mutants defective in the site of gene N product utilization for antitermination of leftward transcription.
    J Mol Biol. 1978 Sep 5;124(1):195-221 PMID: 361968
  2. NusA protein is necessary and sufficient in vitro for phage lambda N gene product to suppress a rho-independent terminator placed downstream of nutL.
    Proc Natl Acad Sci U S A. 1988 Apr;85(8):2494-8 PMID: 2965813
  3. Secondary structure of the leader transcript from the Escherichia coli S10 ribosomal protein operon.
    Nucleic Acids Res. 1988 Sep 26;16(18):8905-24 PMID: 3050893
  4. Genetic analysis of the rnc operon of Escherichia coli.
    J Bacteriol. 1989 May;171(5):2581-90 PMID: 2540151
  5. Unusual mRNA pseudoknot structure is recognized by a protein translational repressor.
    Cell. 1989 May 19;57(4):531-6 PMID: 2470510
  6. HIV-1 TAT "activates" presynthesized RNA in the nucleus.
    Cell. 1989 Jul 28;58(2):269-79 PMID: 2546679
  7. Effects of all single base substitutions in the loop of boxB on antitermination of transcription by bacteriophage lambda's N protein.
    Nucleic Acids Res. 1989 Jul 25;17(14):5565-77 PMID: 2527353
  8. Sequence-specific recognition of RNA hairpins by bacteriophage antiterminators requires a conserved arginine-rich motif.
    Cell. 1989 Oct 6;59(1):207-18 PMID: 2477156
  9. HIV TAR: an RNA enhancer?
    Cell. 1989 Oct 20;59(2):229-30 PMID: 2680105
  10. Target site of Escherichia coli ribosomal protein S15 on its messenger RNA. Conformation and interaction with the protein.
    J Mol Biol. 1990 Jan 20;211(2):415-26 PMID: 2407855
  11. Ribosomal protein L4 stimulates in vitro termination of transcription at a NusA-dependent terminator in the S10 operon leader.
    Proc Natl Acad Sci U S A. 1990 Apr;87(7):2675-9 PMID: 2157208
  12. Integration host factor stimulates the phage lambda pL promoter.
    J Mol Biol. 1990 May 5;213(1):109-21 PMID: 2140136
  13. Transcription elongation and eukaryotic gene regulation.
    Oncogene. 1990 Jun;5(6):777-85 PMID: 2193290
  14. A nuclear translational block imposed by the HIV-1 U3 region is relieved by the Tat-TAR interaction.
    Cell. 1990 Sep 21;62(6):1123-33 PMID: 2205397
  15. Escherichia coli threonyl-tRNA synthetase and tRNA(Thr) modulate the binding of the ribosome to the translational initiation site of the thrS mRNA.
    J Mol Biol. 1990 Nov 20;216(2):299-310 PMID: 2254931
  16. Transcription-dependent competition for a host factor: the function and optimal sequence of the phage lambda boxA transcription antitermination signal.
    Genes Dev. 1990 Dec;4(12A):2210-22 PMID: 2148536
  17. Identification of a T4 gene required for bacteriophage mRNA processing.
    New Biol. 1989 Oct;1(1):54-65 PMID: 2488272
  18. rRNA transcription rate in Escherichia coli.
    J Bacteriol. 1991 Oct;173(20):6647-9 PMID: 1717439
  19. The nut site of bacteriophage lambda is made of RNA and is bound by transcription antitermination factors on the surface of RNA polymerase.
    Genes Dev. 1991 Nov;5(11):2141-51 PMID: 1834523
  20. Ribosomal protein L4 of Escherichia coli: in vitro analysis of L4-mediated attenuation control.
    Biochimie. 1991 Jun;73(6):719-27 PMID: 1764518
  21. Mutations of the phage lambda nutL region that prevent the action of Nun, a site-specific transcription termination factor.
    J Bacteriol. 1992 Mar;174(6):1983-9 PMID: 1532174
  22. Supercoiling, integration host factor, and a dual promoter system, participate in the control of the bacteriophage lambda pL promoter.
    J Mol Biol. 1992 Apr 20;224(4):937-48 PMID: 1533252
  23. RNaselll activation of bacteriophage lambda N synthesis.
    Mol Microbiol. 1991 Dec;5(12):2953-63 PMID: 1839745
  24. Host factor requirements for processive antitermination of transcription and suppression of pausing by the N protein of bacteriophage lambda.
    J Biol Chem. 1992 Sep 25;267(27):19418-26 PMID: 1388170
  25. How the phage lambda N gene product suppresses transcription termination: communication of RNA polymerase with regulatory proteins mediated by signals in nascent RNA.
    J Bacteriol. 1992 Nov;174(21):6711-6 PMID: 1400223
  26. Insertional disruption of the nusB (ssyB) gene leads to cold-sensitive growth of Escherichia coli and suppression of the secY24 mutation.
    Mol Gen Genet. 1992 Sep;234(3):429-32 PMID: 1406588
  27. Recognition of boxA antiterminator RNA by the E. coli antitermination factors NusB and ribosomal protein S10.
    Cell. 1993 Jan 29;72(2):261-8 PMID: 7678781
  28. Ribosome initiation complex formation with the pseudoknotted alpha operon messenger RNA.
    J Mol Biol. 1993 Feb 5;229(3):609-22 PMID: 7679446
  29. Ribosomal protein S15 from Escherichia coli modulates its own translation by trapping the ribosome on the mRNA initiation loading site.
    Proc Natl Acad Sci U S A. 1993 May 15;90(10):4394-8 PMID: 7685101
  30. Transcriptional antitermination.
    Nature. 1993 Jul 29;364(6436):401-6 PMID: 8332211
  31. Control of transcription termination by RNA-binding proteins.
    Annu Rev Biochem. 1993;62:893-930 PMID: 8352604
  32. RNA recognition by the human immunodeficiency virus Tat and Rev proteins.
    Trends Biochem Sci. 1993 Jul;18(7):255-9 PMID: 8212135
  33. Common mechanisms for the control of eukaryotic transcriptional elongation.
    Bioessays. 1993 Oct;15(10):659-65 PMID: 8274141
  34. Bacteriophage lambda N-dependent transcription antitermination. Competition for an RNA site may regulate antitermination.
    J Mol Biol. 1994 Feb 11;236(1):217-28 PMID: 8107107
  35. Regulation of the Bacillus subtilis trp operon by an RNA-binding protein.
    Mol Microbiol. 1994 Mar;11(6):991-7 PMID: 8022289
  36. Conserved structures and diversity of functions of RNA-binding proteins.
    Science. 1994 Jul 29;265(5172):615-21 PMID: 8036511
  37. Control of transcription processivity in phage lambda: Nus factors strengthen the termination-resistant state of RNA polymerase induced by N antiterminator.
    Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8660-4 PMID: 7521531
  38. The bacteriophage T4 regB ribonuclease. Stimulation of the purified enzyme by ribosomal protein S1.
    J Biol Chem. 1994 Oct 28;269(43):26655-62 PMID: 7929399
  39. Enhanced activity of the bacteriophage lambda PL promoter at low temperature.
    Proc Natl Acad Sci U S A. 1995 Mar 14;92(6):2184-8 PMID: 7892244
  40. Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage lambda.
    Proc Natl Acad Sci U S A. 1995 Apr 25;92(9):4061-5 PMID: 7732031
  41. Translation of trpG in Bacillus subtilis is regulated by the trp RNA-binding attenuation protein (TRAP).
    J Bacteriol. 1995 Aug;177(15):4272-8 PMID: 7543470
  42. Tumor suppression and transcription elongation: the dire consequences of changing partners.
    Science. 1995 Sep 8;269(5229):1400-1 PMID: 7660121
  43. trp RNA-binding attenuation protein (TRAP)-trp leader RNA interactions mediate translational as well as transcriptional regulation of the Bacillus subtilis trp operon.
    J Bacteriol. 1995 Nov;177(22):6362-70 PMID: 7592410
  44. A protein-RNA interaction network facilitates the template-independent cooperative assembly on RNA polymerase of a stable antitermination complex containing the lambda N protein.
    Genes Dev. 1995 Nov 15;9(22):2831-45 PMID: 7590257
  45. Bacteriophage lambda N protein alone can induce transcription antitermination in vitro.
    Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):342-6 PMID: 8552635
  46. An RNA polymerase II elongation factor encoded by the human ELL gene.
    Science. 1996 Mar 29;271(5257):1873-6 PMID: 8596958
  47. The N protein of bacteriophage lambda, defined by its DNA sequence, is highly basic.
    Gene. 1979 Dec;8(1):107-19 PMID: 43815
  48. E. coli ribosomal protein L4 is a feedback regulatory protein.
    Cell. 1980 Sep;21(2):517-22 PMID: 6996835
  49. Transcription antitermination by bacteriophage lambda N gene product.
    J Mol Biol. 1980 Jun 15;140(1):57-75 PMID: 6447798
  50. Evidence that ribosomal protein S10 participates in control of transcription termination.
    Proc Natl Acad Sci U S A. 1981 Feb;78(2):1115-8 PMID: 6453343
  51. Protein degradation in E. coli: the lon mutation and bacteriophage lambda N and cII protein stability.
    Cell. 1981 Apr;24(1):225-33 PMID: 6453650
  52. Suppression of transcription termination by phage lambda.
    Science. 1982 May 28;216(4549):946-51 PMID: 6281888
  53. Escherichia coli nusB mutations that suppress nusA1 exhibit lambda N specificity.
    J Mol Biol. 1983 Jul 25;168(1):73-85 PMID: 6224023
  54. Transcription antitermination in vitro by lambda N gene product: requirement for a phage nut site and the products of host nusA, nusB, and nusE genes.
    Cell. 1984 Aug;38(1):165-73 PMID: 6088061
  55. A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors.
    Gene. 1984 Nov;31(1-3):165-71 PMID: 6098521
  56. Bacteriophage lambda N gene leader RNA. RNA processing and translational initiation signals.
    J Biol Chem. 1987 Dec 25;262(36):17651-8 PMID: 2961741
  57. Transcription antitermination: the lambda paradigm updated.
    Mol Microbiol. 1995 Oct;18(2):191-200 PMID: 8709839
  58. A long-range RNA-RNA interaction forms a pseudoknot required for translational control of the IF3-L35-L20 ribosomal protein operon in Escherichia coli.
    EMBO J. 1996 Aug 15;15(16):4402-13 PMID: 8861967
  59. Processing of the major leftward mRNA of coliphage lambda.
    Virology. 1976 May;71(1):262-77 PMID: 1274177
  60. Antitermination and absence of processing of the leftward transcript of coliphage lambda in the RNAase III-deficient host.
    J Mol Biol. 1977 Jan 15;109(2):359-65 PMID: 320345
  61. Independence of gene N and tof functions of bacteriophage lambda.
    J Mol Biol. 1977 Jun 5;112(4):657-60 PMID: 875037
  62. The relationship between function and DNA sequence in an intercistronic regulatory region in phage lambda.
    Nature. 1978 Mar 30;272(5652):414-23 PMID: 634366
  63. The nusA recognition site. Alteration in its sequence or position relative to upstream translation interferes with the action of the N antitermination function of phage lambda.
    J Mol Biol. 1984 Dec 25;180(4):1053-63 PMID: 6098688
  64. Conservation of genome form but not sequence in the transcription antitermination determinants of bacteriophages lambda, phi 21 and P22.
    J Mol Biol. 1985 Jan 5;181(1):75-84 PMID: 3157001
  65. Post-transcriptional regulation accounts for the trans-activation of the human T-lymphotropic virus type III.
    Nature. 1986 Feb 13-19;319(6054):555-9 PMID: 3003584
  66. Suppressors of the secY24 mutation: identification and characterization of additional ssy genes in Escherichia coli.
    J Bacteriol. 1986 Jun;166(3):849-56 PMID: 3011749
  67. Trans-activation of human immunodeficiency virus occurs via a bimodal mechanism.
    Cell. 1986 Sep 26;46(7):973-82 PMID: 3530501
  68. An antitermination protein engages the elongating transcription apparatus at a promoter-proximal recognition site.
    Cell. 1987 Sep 11;50(6):885-99 PMID: 3040263
  69. Autogenous control of the S10 ribosomal protein operon of Escherichia coli: genetic dissection of transcriptional and posttranscriptional regulation.
    Proc Natl Acad Sci U S A. 1987 Sep;84(18):6516-20 PMID: 2442760
  70. lambda N antitermination system: functional analysis of phage interactions with the host NusA protein.
    J Mol Biol. 1987 Apr 20;194(4):679-90 PMID: 2821265
  71. Bacteriophage T4 regA protein binds to mRNAs and prevents translation initiation.
    Proc Natl Acad Sci U S A. 1987 Nov;84(22):7822-6 PMID: 3120177
Article Info
Journal
Genes & development
Abbr.
Genes Dev
ISSN
0890-9369
DOI
10.1101/gad.11.17.2204
Published
1997-09-01
Pages
2204-13
Language
English
Region
United States
NLM ID
8711660
PMCID
PMC275398
Subset
IM
External Links
PubMed source DOI: 10.1101/gad.11.17.2204 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2