Structure and inherent properties of the bacteriophage lambda head shell. III. Spectroscopic studies on the expansion of the prohead.
The head shell of bacteriophage lambda expands by about 20% in diameter when it packages the DNA molecule in vivo. The expansion reaction is essentially a conformational change of the major head protein molecules to a state of lower free energy and can also be triggered in vitro by treatment with 4 M-urea. In order to investigate the conformational change, we have measured the circular dichroism, fluorescence and difference absorption spectra of the lambda head shell before and after the expansion by the treatment with urea. The far-ultraviolet circular dichroism spectra and the fluorescence spectra show that the expansion is not accompanied by a great change in the secondary structure (29% alpha-helix, 23% beta-structure) and the environment (non-polar) of the tryptophan residues of the major head protein molecule. On the other hand, by measurements of the circular dichroism and difference absorption spectra in the near-ultraviolet region as well as by chemical modification experiments with tetranitromethane, we have found that one or two tyrosine residues of the major head protein are transferred from a polar, solvent-exposed to a non-polar, solvent-unexposed environment during the expansion. Judging from these results, the conformational change seems to be mainly intermolecular or interdomainal rather than intradomainal.
D010582:Bacteriophage lambda / Q000032:analysis*; D002942:Circular Dichroism; D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013774:Tetranitromethane / Q000494:pharmacology; D014443:Tyrosine; D014508:Urea / Q000494:pharmacology; D014764:Viral Proteins / Q000032:analysis*
D003432:Cross-Linking Reagents; D014764:Viral Proteins; D014443:Tyrosine; D014508:Urea; D013774:Tetranitromethane