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Volume 272, Number 51, Issue of December 19, 1997
pp. 32108-32114
(Received for publication, June 9, 1997, and in revised form, October 2, 1997)
From the Serine palmitoyltransferase (SPT; EC
2.3.1.50) catalyzes the initial step dedicated to sphingolipid
biosynthesis and is thought to be a key enzyme for regulating cellular
sphingolipid content. For SPT activity, the yeast Saccharomyces
cerevisiae requires two genes, LCB1 and
LCB2. We isolated mammalian LCB1 cDNA
homologs from mouse and Chinese hamster ovary (CHO) cells and an
LCB2 cDNA homolog from CHO cells. The mammalian LCB1
proteins are predicted to have about 35% amino acid identity to the
yeast Lcb1 protein, whereas the CHO LCB2 protein is predicted to have about 40% amino acid identity to the yeast Lcb2 protein. Northern blot
analysis of mRNA isolated from various mouse tissues revealed that
the tissue distribution of both LCB1 and LCB2
messengers followed a similar pattern. Transfection of an SPT-defective
CHO mutant strain with a CHO LCB1-expressing plasmid
restored both SPT activity and de novo sphingolipid
synthesis to the wild type levels, whereas transfection of the mutant
strain with a CHO LCB2-expressing plasmid did not exhibit
any recovery effects, indicating that the SPT defect in the mutant
cells is specifically complemented by the CHO LCB1 homolog.
Furthermore, when the SPT-defective mutant cells were transfected with
a plasmid encoding a His6-tagged CHO LCB1 protein, SPT
activity bound to a Ni2+-immobilized resin. These results
indicate that the CHO LCB1 homolog encodes a component of
SPT.
A Mammalian Homolog of the Yeast LCB1 Encodes a
Component of Serine Palmitoyltransferase, the Enzyme Catalyzing the
First Step in Sphingolipid Synthesis
§
,§
,
,
,
and
Department of Biochemistry and Cell Biology,
National Institute of Infectious Diseases, 1-23-1, Toyama, Shinjuku-ku,
Tokyo 162 Japan, the 
Department of Biochemistry and the Lucille
P. Markey Cancer Center, University of Kentucky Medical Center,
Lexington, Kentucky 40536-0084, and § CREST, Japan Science
and Technology Corporation
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