Production of a functional full-length Xenopus laevis c-Myc protein in insect cells.
C-Myc is a nuclear phosphoprotein whose normal cellular function has not yet been clearly defined. Studies with this protein have always been constrained by the difficulty of obtaining full-length c-Myc in an active form, whatever the expression system used. We report here experimental conditions optimized to increase the solubility and the purification of c-Myc in a baculovirus expression system. Such conditions allow the production of both soluble and active full-length c-Myc. Interestingly, soluble c-Myc is found associated with a 500-kDa high-molecular-mass complex comparable to that found in human and Xenopus laevis embryos, and which may be required for its function in vivo.
Lemaître
J M
JM
Molecular Embryology Unit, Institut Jacques Monod, Paris, France.
Bocquet
S
S
Thierry
N
N
Buckle
R
R
Méchali
M
M
D000818:Animals; D016367:Baculoviridae; D002460:Cell Line; D004622:Embryo, Mammalian; D004625:Embryo, Nonmammalian; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight; D016271:Proto-Oncogene Proteins c-myc / Q000096:biosynthesis* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification; D018411:Spodoptera; D014162:Transfection; D014982:Xenopus laevis
D016271:Proto-Oncogene Proteins c-myc; D011994:Recombinant Proteins