Literature DB >> 2445491

An elongation control particle containing the N gene transcriptional antitermination protein of bacteriophage lambda.

R J Horwitz1, J Li, J Greenblatt.   

Abstract

The N gene transcriptional antitermination protein of bacteriophage lambda is incorporated in vitro into transcriptional elongation complexes containing the E. coli proteins NusA and NusB. The binding of NusA to elongating RNA polymerase is sequence-independent and follows the release of sigma 70. Incorporation of N into the elongation complex requires an N utilization site (nut site) on the DNA template. Incorporation of NusB into the complex requires NusA, ribosomal protein S10, and the boxA component of the nut site. T1 RNAase releases N, but not NusB, from the elongation complex. We therefore propose that an N-modified termination-resistant elongation complex includes an elongation control particle (ECP) containing at least NusA, NusB, S10, N, and an RNA transcript of the nut site.

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Year:  1987        PMID: 2445491     DOI: 10.1016/0092-8674(87)90132-2

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  51 in total

1.  Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination.

Authors:  M Torres; C Condon; J M Balada; C Squires; C L Squires
Journal:  EMBO J       Date:  2001-07-16       Impact factor: 11.598

2.  Structural mimicry in the phage phi21 N peptide-boxB RNA complex.

Authors:  Christopher D Cilley; James R Williamson
Journal:  RNA       Date:  2003-06       Impact factor: 4.942

Review 3.  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

4.  The carboxy-terminal 14 amino acids of phage lambda N protein are dispensable for transcription antitermination.

Authors:  N C Franklin
Journal:  J Bacteriol       Date:  1992-12       Impact factor: 3.490

5.  Sequence-specific Rho-RNA interactions in transcription termination.

Authors:  James E Graham
Journal:  Nucleic Acids Res       Date:  2004-06-04       Impact factor: 16.971

6.  Structural basis for the interaction of Escherichia coli NusA with protein N of phage lambda.

Authors:  Irena Bonin; Rene Mühlberger; Gleb P Bourenkov; Robert Huber; Adelbert Bacher; Gerald Richter; Markus C Wahl
Journal:  Proc Natl Acad Sci U S A       Date:  2004-09-13       Impact factor: 11.205

7.  Mutations of the phage lambda nutL region that prevent the action of Nun, a site-specific transcription termination factor.

Authors:  J Baron; R A Weisberg
Journal:  J Bacteriol       Date:  1992-03       Impact factor: 3.490

8.  Gene Q antiterminator proteins of Escherichia coli phages 82 and lambda suppress pausing by RNA polymerase at a rho-dependent terminator and at other sites.

Authors:  X J Yang; J W Roberts
Journal:  Proc Natl Acad Sci U S A       Date:  1989-07       Impact factor: 11.205

9.  A quantitative description of the binding states and in vitro function of antitermination protein N of bacteriophage lambda.

Authors:  Clarke R Conant; Marc R Van Gilst; Stephen E Weitzel; William A Rees; Peter H von Hippel
Journal:  J Mol Biol       Date:  2005-04-01       Impact factor: 5.469

10.  NusA-stimulated RNA polymerase pausing and termination participates in the Bacillus subtilis trp operon attenuation mechanism invitro.

Authors:  Alexander V Yakhnin; Paul Babitzke
Journal:  Proc Natl Acad Sci U S A       Date:  2002-08-02       Impact factor: 11.205

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