Context and conformation dictate function of a transcription antitermination switch
Data(s) |
2003
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Resumo |
In bacteriophage, transcription elongation is regulated by the N protein, which binds a nascent mRNA hairpin ( termed boxB) and enables RNA polymerase to read through distal terminators. We have examined the structure, energetics and in vivo function of a number of N boxB complexes derived from in vitro protein selection. Trp18 fully stacks on the RNA loop in the wild-type structure, and can become partially or completely unstacked when the sequence context is changed three or four residues away, resulting in a recognition interface in which the best binding residues depend on the sequence context. Notably, in vivo antitermination activity correlates with the presence of a stacked aromatic residue at position 18, but not with N boxB binding affinity. Our work demonstrates that RNA polymerase responds to subtle conformational changes in cis-acting regulatory complexes and that approximation of components is not sufficient to generate a fully functional transcription switch. |
Identificador | |
Idioma(s) |
英语 |
Fonte |
Xia TB;Frankel A;Takahashi TT;Ren JS;Roberts RW.Context and conformation dictate function of a transcription antitermination switch,NATURE STRUCTURAL BIOLOGY,2003,10(10):812-819 |
Palavras-Chave | #RNA-BINDING PEPTIDES #LAMBDA-N-PROTEIN #PHAGE-LAMBDA #BACTERIOPHAGE-LAMBDA #PROCESSIVE ANTITERMINATION #GENE-EXPRESSION #IN-VITRO #COMPLEX #POLYMERASE #ELONGATION |
Tipo |
期刊论文 |