INDEPENDENT LIGAND-INDUCED FOLDING OF THE RNA-BINDING DOMAIN AND 2 FUNCTIONALLY DISTINCT ANTITERMINATION REGIONS IN THE PHAGE-LAMBDA N-PROTEIN

Citation
J. Mogridge et al., INDEPENDENT LIGAND-INDUCED FOLDING OF THE RNA-BINDING DOMAIN AND 2 FUNCTIONALLY DISTINCT ANTITERMINATION REGIONS IN THE PHAGE-LAMBDA N-PROTEIN, MOLECULAR CELL, 1(2), 1998, pp. 265-275
Citations number
57
Categorie Soggetti
Cell Biology","Engineering, Eletrical & Electronic
Journal title
ISSN journal
10972765
Volume
1
Issue
2
Year of publication
1998
Pages
265 - 275
Database
ISI
SICI code
1097-2765(1998)1:2<265:ILFOTR>2.0.ZU;2-3
Abstract
The transcriptional antitermination protein N of bacteriophage lambda binds the boxB component of the RNA enhancer nut (boxA + boxB) and the E. coli elongation factor NusA. Efficient antitermination by N requir es an RNA-binding domain (amino acids 1-22) and two activating regions for antitermination: a newly identified NusA-binding region (amino ac ids 34-47) that suppresses NusA's enhancement of termination, and a ca rboxy-terminal region (amino acids 73-107) that interacts directly wit h RNA polymerase. Heteronuclear magnetic resonance experiments demonst rate that N is a disordered protein. Interaction with boxB RNA induces only the RNA-binding domain of N to adopt a folded conformation, whil e the activating regions of the protein remain disordered in the absen ce of their target proteins.