By the same authors

From the same journal

The crystal structure of NusB from Mycobacterium tuberculosis

Research output: Contribution to journalArticle

Author(s)

  • B Gopal
  • L F Haire
  • R A Cox
  • M J Colston
  • S Major
  • J A Brannigan
  • S J Smerdon
  • G Dodson

Department/unit(s)

Publication details

JournalNature Structural Biology
DatePublished - Jun 2000
Issue number6
Volume7
Number of pages4
Pages (from-to)475-478
Original languageEnglish

Abstract

Both prokaryotes and eukaryotes regulate transcription through mechanisms that suppress termination signals. An antitermination mechanism was first characterized in bacteriophage lambda. Bacteria have analogous machinery that regulates ribosomal RNA transcription and employs host factors, called the N-utilizing (where N stands for the phage lambda N protein) substances (Nus), NusA, NusB, NusE and NusG. Here we report the crystal structure of NusB from Mycobacterium tuberculosis, the bacterium that causes tuberculosis in humans. This molecule shares a similar tertiary structure with the related Escherichia coliprotein but adopts a different quaternary organization. We show that, unlike the E. coli homolog, M. tuberculosis NusB is dimeric both in solution and in the crystal. These data help provide a framework for understanding the structural and biological function of NusB in the prokaryotic transcriptional antitermination complex.

    Research areas

  • RIBOSOMAL-RNA, ESCHERICHIA-COLI, PROTEIN MODELS, ANTITERMINATION, TRANSCRIPTION, RECOGNITION, REFINEMENT, COMPLEX, GENOME, MOTIF

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