The r i n gene of S. ci n risiat encode ,r protein, l-'at 1 p, which represents ihr hnmoiogiie of the mammalian fatty acid transport protein FAT P. Strains containing a deletion in KAT1 (fall} are compromised in their ability to transport exogenous long-chain fatly at ids. This results in an inability to grow under anaerolm conditions and under conditions where fatty acid synthesis is inhibited either by mutation tir by ( emlenin. rr'e have construcîed a yeast expression plasmid YpDBlO'l containing the murine FATP <DNA under the control of the glvreraldi'hyde 3-phosphate dehydrogenase promoter to evaluate whether the m urine gene is able to complement tin1 yeast jat t strain. As controls, we used the FA !'! gene in Ypl)B10'2 and the venor control YpBB35S also transformed mlo the fatf >train. As rxpf-ctpd Ypl)B102 resiores the rapacity of the rw strain tu Iransport exogenous lon-4rtiain fatty acids; to grow under anaerobic conditions in media siippac-mrted with fatly acids; and under conditionswhrre tat TV acid synthesis is cornpromW'd upon fatty acid supplementation. Of pariiniiai interest. huwev.T. was the finding that YpDBlO't was also ablo tu conipl'-meiil the fat ! mutation- We have also monitored complementation uMne confocal microscopy and the fluorescent Song chain fatty acid HODIPY3-42-i. i he>e results dramatically il lust ïa te complementation of 1 he veast fdt ! si rain by 1hr inurine FAT P. This work, i herefore provides a foundation for additional work investigating the rnechani.-tns that govern fatty acid transport in 'ik.trvo! t v-4iems hy n-4ine, the veast .t- a niodel -4ystem.
|Original language||English (US)|
|State||Published - 1998|
ASJC Scopus subject areas
- Molecular Biology