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首页> 外文期刊>Molecular and Cellular Biology >Formation of the peroxisome lumen is abolished by loss of Pichia pastoris Pas7p, a zinc-binding integral membrane protein of the peroxisome.
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Formation of the peroxisome lumen is abolished by loss of Pichia pastoris Pas7p, a zinc-binding integral membrane protein of the peroxisome.

机译：过氧化物酶体腔的形成被毕赤酵母Pas7p（过氧化物酶体的锌结合性整合膜蛋白）的丧失所消除。

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We have cloned and sequenced PAS7, a gene required for peroxisome assembly in the yeast Pichia pastoris. The product of this gene, Pas7p, is a member of the C3HC4 superfamily of zinc-binding proteins. Point mutations that alter conserved residues of the C3HC4 motif abolish PAS7 activity and reduce zinc binding, suggesting that Pas7p binds zinc in vivo and that zinc binding is essential for PAS7 function. As with most pas mutants, pas7 cells exhibit a pronounced deficiency in import of peroxisomal matrix proteins that contain either the type 1 peroxisomal targeting signal (PTS1) or the type 2 PTS (PTS2). However, while other yeast and mammalian pas mutants accumulate ovoid, vesicular peroxisomal intermediates, loss of Pas7p leads to accumulation of membrane sheets and vesicles which lack a recognizable lumen. Thus, Pas7p appears to be essential for protein translocation into peroxisomes as well as formation of the lumen of the organelle. Consistent with these data, we find that Pas7p is an integral peroxisomal membrane protein which is entirely resistant to exogenous protease and thus appears to reside completely within the peroxisome. Our observations suggest that the function of Pas7p defines a previously unrecognized step in peroxisome assembly: formation of the peroxisome lumen. Furthermore, because the peroxisomal intermediates in the pas7 delta mutant proliferate in response to peroxisome-inducing environmental conditions, we conclude that Pas7p is not required for peroxisome proliferation.
机译：我们已经克隆并测序了PAS7，这是酵母毕赤酵母中过氧化物酶体装配所需的基因。该基因的产物Pas7p是锌结合蛋白C3HC4超家族的成员。改变C3HC4基序的保守残基的点突变消除了PAS7的活性并减少了锌的结合，这表明Pas7p在体内结合了锌，并且锌的结合对于PAS7的功能至关重要。与大多数pas突变体一样，pas7细胞在过氧化物酶体基质蛋白的输入中表现出明显的缺陷，该蛋白含有1型过氧化物酶体靶向信号（PTS1）或2型PTS（PTS2）。然而，尽管其他酵母和哺乳动物的pas突变体会积聚卵形，囊泡过氧化物酶体中间体，但Pas7p的缺失会导致缺乏可识别内腔的膜片和囊泡积聚。因此，Pas7p似乎对于蛋白质易位到过氧化物酶体以及细胞器内腔的形成至关重要。与这些数据一致，我们发现Pas7p是完整的过氧化物酶体膜蛋白，其完全抗外源蛋白酶，因此似乎完全存在于过氧化物酶体中。我们的观察结果表明，Pas7p的功能定义了过氧化物酶体装配中以前无法识别的步骤：过氧化物酶体腔的形成。此外，由于pas7 delta突变体中的过氧化物酶体中间体响应过氧化物酶体诱导的环境条件而增殖，因此我们得出结论，过氧化物酶体增殖不需要Pas7p。

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