Literature DB >> 7730297

Structural and functional analyses of the transcription-translation proteins NusB and NusE.

D L Court1, T A Patterson, T Baker, N Costantino, X Mao, D I Friedman.   

Abstract

The NusB and NusE (ribosomal protein S10) proteins function in transcription and translation. The two proteins form a complex that binds to the boxA sequence found in the leader RNA of rrn operons; boxA is required for transcription antitermination in rrn operons. Although binding of these two proteins to the boxA RNA of the bacteriophage lambda nut site has not been observed, both NusB and NusE as well as the RNA boxA sequence are required for lambda N-mediated antitermination. Studies identifying the amino acid changes caused by mutations in nusB and nusE and relating these changes to altered function are reported. It is concluded that boxA is essential for an effective NusB contribution to N-mediated antitermination and that by mutation NusB may be changed to allow more-effective binding to boxA variants.

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Year:  1995        PMID: 7730297      PMCID: PMC176924          DOI: 10.1128/jb.177.9.2589-2591.1995

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  22 in total

Review 1.  How the phage lambda N gene product suppresses transcription termination: communication of RNA polymerase with regulatory proteins mediated by signals in nascent RNA.

Authors:  A Das
Journal:  J Bacteriol       Date:  1992-11       Impact factor: 3.490

2.  Insertional disruption of the nusB (ssyB) gene leads to cold-sensitive growth of Escherichia coli and suppression of the secY24 mutation.

Authors:  T Taura; C Ueguchi; K Shiba; K Ito
Journal:  Mol Gen Genet       Date:  1992-09

3.  Transcription-dependent competition for a host factor: the function and optimal sequence of the phage lambda boxA transcription antitermination signal.

Authors:  D I Friedman; E R Olson; L L Johnson; D Alessi; M G Craven
Journal:  Genes Dev       Date:  1990-12       Impact factor: 11.361

4.  Suppressors of the secY24 mutation: identification and characterization of additional ssy genes in Escherichia coli.

Authors:  K Shiba; K Ito; T Yura
Journal:  J Bacteriol       Date:  1986-06       Impact factor: 3.490

5.  Sequence-specific recognition of RNA hairpins by bacteriophage antiterminators requires a conserved arginine-rich motif.

Authors:  D Lazinski; E Grzadzielska; A Das
Journal:  Cell       Date:  1989-10-06       Impact factor: 41.582

6.  Conservation of genome form but not sequence in the transcription antitermination determinants of bacteriophages lambda, phi 21 and P22.

Authors:  N C Franklin
Journal:  J Mol Biol       Date:  1985-01-05       Impact factor: 5.469

Review 7.  RNA and protein elements of E. coli and lambda transcription antitermination complexes.

Authors:  J W Roberts
Journal:  Cell       Date:  1993-03-12       Impact factor: 41.582

Review 8.  Transcriptional antitermination.

Authors:  J Greenblatt; J R Nodwell; S W Mason
Journal:  Nature       Date:  1993-07-29       Impact factor: 49.962

9.  Bacteriophage lambda N-dependent transcription antitermination. Competition for an RNA site may regulate antitermination.

Authors:  T A Patterson; Z Zhang; T Baker; L L Johnson; D I Friedman; D L Court
Journal:  J Mol Biol       Date:  1994-02-11       Impact factor: 5.469

10.  Recognition of boxA antiterminator RNA by the E. coli antitermination factors NusB and ribosomal protein S10.

Authors:  J R Nodwell; J Greenblatt
Journal:  Cell       Date:  1993-01-29       Impact factor: 41.582

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  15 in total

Review 1.  Mapping the bacterial cell architecture into the chromosome.

Authors:  A Danchin; P Guerdoux-Jamet; I Moszer; P Nitschké
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2000-02-29       Impact factor: 6.237

Review 2.  A new look at bacteriophage lambda genetic networks.

Authors:  Donald L Court; Amos B Oppenheim; Sankar L Adhya
Journal:  J Bacteriol       Date:  2006-11-03       Impact factor: 3.490

3.  Structural biophysics of the NusB:NusE antitermination complex.

Authors:  Ranabir Das; Sandra Loss; Jess Li; David S Waugh; Sergey Tarasov; Paul T Wingfield; R Andrew Byrd; Amanda S Altieri
Journal:  J Mol Biol       Date:  2007-11-17       Impact factor: 5.469

4.  Structural and functional analysis of the E. coli NusB-S10 transcription antitermination complex.

Authors:  Xiao Luo; He-Hsuan Hsiao; Mikhail Bubunenko; Gert Weber; Donald L Court; Max E Gottesman; Henning Urlaub; Markus C Wahl
Journal:  Mol Cell       Date:  2008-12-26       Impact factor: 17.970

5.  Loss of overproduction of polypeptide release factor 3 influences expression of the tryptophanase operon of Escherichia coli.

Authors:  C Yanofsky; V Horn; Y Nakamura
Journal:  J Bacteriol       Date:  1996-07       Impact factor: 3.490

Review 6.  Linkage map of Escherichia coli K-12, edition 10: the traditional map.

Authors:  M K Berlyn
Journal:  Microbiol Mol Biol Rev       Date:  1998-09       Impact factor: 11.056

7.  Escherichia coli transcription factor NusG binds to 70S ribosomes.

Authors:  Shivalika Saxena; Kamila K Myka; Robert Washburn; Nina Costantino; Donald L Court; Max E Gottesman
Journal:  Mol Microbiol       Date:  2018-04-06       Impact factor: 3.501

8.  Crystal structures of the antitermination factor NusB from Thermotoga maritima and implications for RNA binding.

Authors:  Irena Bonin; Rudolf Robelek; Heike Benecke; Henning Urlaub; Adelbert Bacher; Gerald Richter; Markus C Wahl
Journal:  Biochem J       Date:  2004-11-01       Impact factor: 3.857

9.  Evolutionary comparison of ribosomal operon antitermination function.

Authors:  Kristine B Arnvig; Shirley Zeng; Selwyn Quan; Alexander Papageorge; Ning Zhang; Anuradha C Villapakkam; Catherine L Squires
Journal:  J Bacteriol       Date:  2008-08-29       Impact factor: 3.490

10.  Fine tuning of the E. coli NusB:NusE complex affinity to BoxA RNA is required for processive antitermination.

Authors:  Björn M Burmann; Xiao Luo; Paul Rösch; Markus C Wahl; Max E Gottesman
Journal:  Nucleic Acids Res       Date:  2009-10-23       Impact factor: 16.971

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