Structural and thermodynamic characteristics of the binding of the lambda N protein to a RNA hairpin.
The specific binding of the lambda N protein to a 15 nucleotide RNA oligomer that forms a hairpin structure has been investigated by biophysical methods. Using fluorescence spectroscopy and equilibrium ultra-centrifugation, it was found that the N protein binds specifically to this RNA hairpin as a monomer. Circular dichroism experiments show that both the N protein and the RNA hairpin undergo structural change upon association of the complex.
Van Gilst
M
M
Department of Chemistry, University of Oregon, Eugene 97403, USA.
Rees
W A
WA
von Hippel
P H
PH
D010582:Bacteriophage lambda / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D001665:Binding Sites; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D012367:RNA, Viral / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013816:Thermodynamics; D054334:Viral Regulatory and Accessory Proteins / Q000737:chemistry / Q000378:metabolism*
C059417:N protein, Bacteriophage lambda; D012367:RNA, Viral; D054334:Viral Regulatory and Accessory Proteins