IDENTIFICATION OF PEROXISOMAL TARGETING SIGNALS LOCATED AT THE CARBOXY TERMINUS OF 4 PEROXISOMAL PROTEINS

IDENTIFICATION OF PEROXISOMAL TARGETING SIGNALS LOCATED AT THE CARBOXY TERMINUS OF 4 PEROXISOMAL PROTEINS
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DOI:
10.1083/jcb.107.3.897
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发表时间:
1988-09-01
影响因子:
7.8
通讯作者:
SUBRAMANI, S
SUBRAMANI, S
中科院分区:
生物学1区
文献类型:
--
作者:
GOULD, SJ;KELLER, GA;SUBRAMANI, S

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为了了解蛋白质是如何被导入到过氧化酶体中的,我们试图确定四种不相关的过氧化物体蛋白中的过氧化物体靶向信号:人过氧化氢酶、大鼠水合酶:脱氢酶、猪D-氨基酸氧化酶和大鼠酰辅酶A氧化酶。通过基因融合实验,我们已经确定了每个蛋白质的一个区域,该区域可以将异源蛋白质定向到过氧化物体。在每种情况下,过氧化体靶向信号都包含在蛋白质的羧基末端或其附近。对于过氧化氢酶,过氧化物体靶向信号位于蛋白质的COOH末端27个氨基酸内。对于水合酶:脱氢酶、D-氨基酸氧化酶和酰基辅酶A氧化酶,靶向信号分别位于15、14和15个氨基酸的羧基末端。序列Ser-Lys/His-Leu的三肽存在于每个这些靶向信号中以及在萤火虫荧光素酶(Gould,S.J.,G.-A.Keller和S.Subramani)中鉴定的过氧体靶向信号中。1987年。J.细胞生物学。105:2923-2931)。当水合酶的过氧化体靶向信号:脱氢酶发生突变,使Ser-Lys-Leu三肽转变为Ser-Asn-Leu时,它不再能将蛋白质定向到过氧酶体上。我们认为该三肽是至少一类过氧化体靶向信号的基本元件。
As part of an effort to understand how proteins are imported into the peroxisome, we have sought to identify the peroxisomal targeting signals in four unrelated peroxisomal proteins: human catalase, rat hydratase:dehydrogenase, pig D-amino acid oxidase, and rat acyl-CoA oxidase. Using gene fusion experiments, we have identified a region of each protein that can direct heterologous proteins to peroxisomes. In each case, the peroxisomal targeting signal is contained at or near the carboxy terminus of the protein. For catalase, the peroxisomal targeting signal is located within the COOH-terminal 27 amino acids of the protein. For hydratase:dehydrogenase, D-amino acid oxidase, and acyl-CoA oxidase, the targeting signals are located within the carboxy-terminal 15, 14, and 15 amino acids, respectively. A tripeptide of the sequence Ser-Lys/His-Leu is present in each of these targeting signals as well as in the peroxisomal targeting signal identified in firefly luciferase (Gould, S. J., G.-A. Keller, and S. Subramani. 1987. J. Cell Biol. 105:2923-2931). When the peroxisomal targeting signal of the hydratase:dehydrogenase is mutated so that the Ser-Lys-Leu tripeptide is converted to Ser-Asn-Leu, it can no longer direct proteins to peroxisomes. We suggest that this tripeptide is an essential element of at least one class of peroxisomal targeting signals.