Localization of the membrane-associated region of vesicular stomatitis virus M protein at the N terminus, using the hydrophobic, photoreactive probe 125I-TID.
The membrane-reactive, photoactivatable probe 125I-TID [3-(trifluoromethyl)-3-(m-[125I]iodophenyl)-3H-diazirine] was found to label the M protein of vesicular stomatitis virus about 40% as much as G protein in intact virions, in agreement with labeling studies with other probes. By analyzing limited tryptic digestion and specific chemical cleavage products, the label was essentially entirely localized within the first 19, and probably within the first 5 to 10, amino acid residues at the N terminus, identifying this short amphipathic segment as the likely site of interaction of M protein with the viral bilayer.
Lenard
J
J
Department of Physiology and Biophysics, Robert Wood Johnson Medical School, University of Medicine and Dentistry, New Jersey, Piscataway 08854-5635.
Vanderoef
R
R
D000595:Amino Acid Sequence; D000818:Animals; D001389:Azirines; D001665:Binding Sites; D006224:Cricetinae; D005561:Formates; D008565:Membrane Proteins / Q000648:ultrastructure*; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010777:Photochemistry; D012995:Solubility; D014357:Trypsin; D014721:Vesicular stomatitis Indiana virus / Q000648:ultrastructure*; D014763:Viral Matrix Proteins / Q000648:ultrastructure*
D001389:Azirines; D005561:Formates; D008565:Membrane Proteins; D014763:Viral Matrix Proteins; C030544:formic acid; C033174:3-(trifluoromethyl)-3-(3-iodophenyl)diazirine; D014357:Trypsin