Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein

Mol Cell. 1998 Jan;1(2):265-75. doi: 10.1016/s1097-2765(00)80027-1.

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 requires an RNA-binding domain (amino acids 1-22) and two activating regions for antitermination: a newly identified NusA-binding region (amino acids 34-47) that suppresses NusA's enhancement of termination, and a carboxy-terminal region (amino acids 73-107) that interacts directly with RNA polymerase. Heteronuclear magnetic resonance experiments demonstrate that N is a disordered protein. Interaction with boxB RNA induces only the RNA-binding domain of N to adopt a folded conformation, while the activating regions of the protein remain disordered in the absence of their target proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Bacteriophage lambda / chemistry*
  • Bacteriophage lambda / enzymology
  • Bacteriophage lambda / genetics*
  • Binding Sites / physiology
  • DNA-Directed RNA Polymerases / metabolism
  • Enhancer Elements, Genetic / physiology
  • Escherichia coli Proteins
  • Gene Expression Regulation, Viral*
  • Ligands
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Peptide Elongation Factors*
  • Peptide Fragments / metabolism
  • Protein Structure, Tertiary
  • RNA, Viral / chemistry
  • RNA, Viral / genetics
  • RNA, Viral / metabolism
  • Regulatory Sequences, Nucleic Acid
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism
  • Transcriptional Elongation Factors
  • Viral Regulatory and Accessory Proteins / chemistry*
  • Viral Regulatory and Accessory Proteins / genetics
  • Viral Regulatory and Accessory Proteins / metabolism*

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Ligands
  • N protein, Bacteriophage lambda
  • Peptide Elongation Factors
  • Peptide Fragments
  • RNA, Viral
  • Transcription Factors
  • Transcriptional Elongation Factors
  • Viral Regulatory and Accessory Proteins
  • nusA protein, E coli
  • DNA-Directed RNA Polymerases