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Structural basis for RNA recognition by NusB and NusE in the initiation of transcription antitermination

  1. Author:
    Stagno, J. R.
    Altieri, A. S.
    Bubunenko, M.
    Tarasov, S. G.
    Li, J.
    Court, D. L.
    Byrd, R. A.
    Ji, X. H.

  2. Author Address

    [Stagno, JR; Ji, XH] SAIC Frederick Inc, Lab Macromol Crystallog, Frederick, MD 21702 USA. [Altieri, AS; Tarasov, SG; Li, J; Byrd, RA] SAIC Frederick Inc, Struct Biophys Lab, Frederick, MD 21702 USA. [Bubunenko, M; Court, DL] SAIC Frederick Inc, Gene Regulat & Chromosome Biol Lab, Frederick, MD 21702 USA. [Bubunenko, M] SAIC Frederick Inc, Basic Res Program, Frederick, MD 21702 USA. NCI, Frederick, MD 21702 USA.;Ji, XH (reprint author), SAIC Frederick Inc, Lab Macromol Crystallog, Frederick, MD 21702 USA;jix@mail.nih.gov
    1. Year: 2011
    2. Date: Sep
  2. Journal: Nucleic Acids Research
    1. 39
    2. 17
    3. Pages: 7803-7815
  4. Type of Article: Article
  5. ISSN: 0305-1048
  1. Abstract:

    Processive transcription antitermination requires the assembly of the complete antitermination complex, which is initiated by the formation of the ternary NusB-NusE-BoxA RNA complex. We have elucidated the crystal structure of this complex, demonstrating that the BoxA RNA is composed of 8 nt that are recognized by the NusB-NusE heterodimer. Functional biologic and biophysical data support the structural observations and establish the relative significance of key protein-protein and protein-RNA interactions. Further crystallographic investigation of a NusB-NusE-dsRNA complex reveals a heretofore unobserved dsRNA binding site contiguous with the BoxA binding site. We propose that the observed dsRNA represents BoxB RNA, as both single-stranded BoxA and double-stranded BoxB components are present in the classical lambda antitermination site. Combining these data with known interactions amongst antitermination factors suggests a specific model for the assembly of the complete antitermination complex.

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External Sources

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  2. DOI: 10.1093/nar/gkr418
  3. View record in Web of Science®
  4. WOS: 000295184800044

Library Notes

  1. Fiscal Year: FY2011-2012
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