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J. Biol. Chem., Vol. 265, Issue 17, 10109-10117, Jun, 1990
DO Clary and JE Rothman
We report conditions under which Golgi membranes depleted of peripheral
membrane proteins can be reconstituted for intra-cisternal vesicular
transport. Analysis of the reconstitution reveals requirements for N-
ethylmaleimide-sensitive fusion protein, a purified peripheral protein
involved in the fusion stage of vesicular transport, as well as other
peripheral protein activities which can be provided by mammalian cytosol
but not yeast cytosol. The restorative activity in bovine brain cytosol is
found in two broad and complementing fractions, of average native molecular
masses of about 500 and 40 kDa, termed Fr1 and Fr2, respectively. This
resolved transport system was used to develop a purification scheme for
Fr2. Three proteins of apparent molecular masses of 35, 36, and 39 kDa
(Fr2-alpha, -beta, and -gamma, respectively) were found to be responsible
for Fr2 activity and were purified to homogeneity. Each Fr2 protein has
activity by itself in the reconstituted in vitro Golgi transport assay,
although each exhibits a different specific activity and plateau value. No
synergy of the three Fr2 proteins was observed during mixing experiments.
The three Fr2 proteins seem to be closely related based on size, in vitro
activities, chromatographic properties, and peptide maps and may comprise a
new family of proteins involved in vesicular transport.
Purification of three related peripheral membrane proteins needed for vesicular transport
Department of Biology, Princeton University, New Jersey 08544.
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