A Saccharomyces cerevisiae gene required for heterologous fatty acid elongase activity encodes a microsomal β-keto-reductase

A Saccharomyces cerevisiae gene required for heterologous fatty acid elongase activity encodes a microsomal β-keto-reductase
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DOI:
10.1074/jbc.m111441200
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发表时间:
2002-03-29
影响因子:
4.8
通讯作者:
Napier, JA
Napier, JA
中科院分区:
生物学2区
文献类型:
--
作者:
Beaudoin, F;Gable, K;Napier, JA

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一些酿酒酵母膜结合的氧化还原酶的微粒体脂肪酸延伸的潜在作用进行了研究,通过测定异源延伸活动在个别缺失突变体。一个酵母基因YBR 159 w被鉴定为秀丽隐杆线虫延伸酶PEA 1(F56 H11.4)和拟南芥延伸酶FAE 1两者的活性所需。Ybr 159 p与人类类固醇脱氢酶具有有限的同源性,是短链醇脱氢酶超家族的成员。与以前的报道相反,YBR 159 w的破坏是不致命的,尽管突变体生长缓慢并且显示出高的温度敏感性。Ybr 159 p和拟南芥同源物被证明恢复异源延长酶活性时,在ybr 159 Delta突变体中表达。ybr 159 Delta细胞的微粒体制备物的生化表征揭示了β-酮酰基还原的主要扰动,证实了YBR 159 w作为微粒体延伸酶的编码组分的分配。
A number of Saccharomyces cerevisiae membrane-bound oxidoreductases were examined for potential roles in microsomal fatty acid elongation, by assaying heterologous elongating activities in individual deletion mutants. One yeast gene, YBR159w, was identified as being required for activity of both the Caenorhabditis elegans elongase PEA1 (F56H11.4) and the Arabidopsis thaliana elongase FAE1. Ybr159p shows some limited homology to human steroid dehydrogenases and is a member of the short-chain alcohol dehydrogenase superfamily. Disruption of YBR159w is not lethal, in contrast to previous reports, although the mutants are slow growing and display high temperature sensitivity. Both Ybr159p and an Arabidopsis homologue were shown to restore heterologous elongase activities when expressed in ybr159Delta mutants. Biochemical characterization of microsomal preparations from ybr159Delta cells revealed a primary perturbation in beta-ketoacyl reduction, confirming the assignment of YBR159w as encoding a component of the microsomal elongase.