Journal
NUCLEIC ACIDS RESEARCH
Volume 39, Issue 17, Pages 7803-7815Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkr418
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Funding
- US Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]
- National Institutes of Health, National Cancer Institute, Center for Cancer Research
- National Institute of Allergy and Infectious Diseases
- National Cancer Institute, National Institutes of Health [N01-CO-12400]
- National Institutes of Health Intramural Research
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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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