
Structural and functional analyses of the transcription-translation proteins NusB and NusE
Author(s) -
Donald L. Court,
Thomas Patterson,
Teresa Baker,
Nina Costantino,
Xiahong Mao,
David I. Friedman
Publication year - 1995
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.177.9.2589-2591.1995
Subject(s) - antitermination , biology , operon , transcription (linguistics) , genetics , rna , ribosomal rna , ribosomal protein , gene , ribosome , escherichia coli , linguistics , philosophy
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.