Cleavage of vesicular stomatitis virus matrix protein prevents self-association and leads to crystallization.
The matrix protein (M) of vesicular stomatitis virus is responsible for the budding of newly formed virions out of host cells. In vitro, it has been shown to self-associate, a property that may be related to the role of M in virus assembly but also prevents crystallization. Using limited proteolysis by thermolysin, we have isolated and characterized two soluble fragments of the protein that remain noncovalently associated. The digestion product does not self-associate nor is it recruited in aggregates formed by intact M molecules. These results identify a peptide, located at the surface of the protein and disorganized by thermolysin cleavage, responsible for M self-association. The thermolysin-resistant core of M has been crystallized and the crystals diffract to 2-A resolution.
Gaudier
M
M
Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91198 Gif sur Yvette Cedex, France.
Gaudin
Y
Y
Knossow
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D003460:Crystallization; D010450:Endopeptidases / Q000378:metabolism; D008969:Molecular Sequence Data; D013820:Thermolysin / Q000378:metabolism; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism*; D014763:Viral Matrix Proteins / Q000378:metabolism*
C094460:M protein, Vesicular stomatitis virus; D014763:Viral Matrix Proteins; D010450:Endopeptidases; D013820:Thermolysin