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Vol. 13, Issue 5, 1484-1500, May 2002
and
*Department of Biology, Massachusetts Institute of Technology,
Cambridge, Massachusetts 02139; and The Saccharomyces cerevisiae proteins Sec34p and
Sec35p are components of a large cytosolic complex involved in protein
transport through the secretory pathway. Characterization of a new
secretion mutant led us to identify SEC36, which encodes
a new component of this complex. Sec36p binds to Sec34p and Sec35p, and
mutation of SEC36 disrupts the complex, as determined by
gel filtration. Missense mutations of SEC36 are lethal
with mutations in COPI subunits, indicating a functional connection
between the Sec34p/sec35p complex and the COPI vesicle coat. Affinity
purification of proteins that bind to Sec35p-myc allowed identification
of two additional proteins in the complex. We call these two conserved
proteins Sec37p and Sec38p. Disruption of either SEC37
or SEC38 affects the size of the complex that contains
Sec34p and Sec35p. We also examined COD4,
COD5, and DOR1, three genes recently
reported to encode proteins that bind to Sec35p. Each of the eight
genes that encode components of the Sec34p/sec35p complex was tested
for its contribution to cell growth, protein transport, and the
integrity of the complex. These tests indicate two general types of
subunits: Sec34p, Sec35p, Sec36p, and Sec38p seem to form the essential core of a complex to which Sec37p, Cod4p, Cod5p, and Dor1p seem to be
peripherally attached.
Department of Cell
Biology, Albert Einstein College of Medicine, Bronx, New York 10461
Present address: Institute of Molecular
and Cell Biology, National University of Singapore, Singapore 117609.
§
Corresponding author. E-mail address:
ckaiser{at}mit.edu.
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