Origin and evolution of the peroxisomal proteome.
Origin and evolution of the peroxisomal proteome.
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DOI：
10.1186/1745-6150-1-8
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发表时间：
2006-03-23
期刊：
影响因子：
5.5
通讯作者：
Huynen, Martijn A.
中科院分区：
文献类型：
--
作者：
Gabaldon, Toni;Snel, Berend;van Zimmeren, Frank;Hemrika, Wieger;Tabak, Henk;Huynen, Martijn A.
过氧化物酶体是真核生物中普遍存在的细胞器，参与各种氧化反应。它们的酶含量因物种而异，但共同的蛋白质输入和细胞器生物发生系统的存在支持单一的进化起源。然而，这一起源的确切情况仍有待确定。像线粒体和叶绿体一样，过氧化物酶体在翻译后分裂和输入蛋白质的能力支持内共生起源。然而，这一观点受到了最近发现的挑战，突变的，缺乏过氧化物酶体的细胞在引入野生型基因后恢复过氧化物酶体，并且过氧化物酶体是由内质网形成的。由于缺乏过氧化物酶体基因组，因此无法像对线粒体或叶绿体进行经典分析那样解决争论。因此，我们对酵母和大鼠过氧化物酶体蛋白质组进行了大规模的系统发育分析。我们的研究结果表明，大多数过氧化物酶体蛋白（39-58%）是真核来源的，包括所有参与细胞器生物发生或维持的蛋白质。很大一部分（13-18%）主要由酶组成，起源于α -变形菌，似乎是最初靶向线粒体的蛋白质募集的结果。与过氧化物酶体在内质网中形成的发现一致，我们发现最普遍保守的过氧化物酶体生物发生和维持蛋白与内质网辅助衰变途径的蛋白同源。总之，我们的结果表明，过氧化物酶体不具有内共生起源，其蛋白质是从原始真核生物中存在的池中招募的。此外，原始过氧化物酶体蛋白质组的重建表明，在个体发育和系统发育上，过氧化物酶体起源于内质网。本文由arady Mushegian， Gáspar j<s:1>凯利和John Logsdon审阅。对于完整的评论，请转到评论者的评论部分。
Peroxisomes are ubiquitous eukaryotic organelles involved in various oxidative reactions. Their enzymatic content varies between species, but the presence of common protein import and organelle biogenesis systems support a single evolutionary origin. The precise scenario for this origin remains however to be established. The ability of peroxisomes to divide and import proteins post-translationally, just like mitochondria and chloroplasts, supports an endosymbiotic origin. However, this view has been challenged by recent discoveries that mutant, peroxisome-less cells restore peroxisomes upon introduction of the wild-type gene, and that peroxisomes are formed from the Endoplasmic Reticulum. The lack of a peroxisomal genome precludes the use of classical analyses, as those performed with mitochondria or chloroplasts, to settle the debate. We therefore conducted large-scale phylogenetic analyses of the yeast and rat peroxisomal proteomes. Our results show that most peroxisomal proteins (39–58%) are of eukaryotic origin, comprising all proteins involved in organelle biogenesis or maintenance. A significant fraction (13–18%), consisting mainly of enzymes, has an alpha-proteobacterial origin and appears to be the result of the recruitment of proteins originally targeted to mitochondria. Consistent with the findings that peroxisomes are formed in the Endoplasmic Reticulum, we find that the most universally conserved Peroxisome biogenesis and maintenance proteins are homologous to proteins from the Endoplasmic Reticulum Assisted Decay pathway. Altogether our results indicate that the peroxisome does not have an endosymbiotic origin and that its proteins were recruited from pools existing within the primitive eukaryote. Moreover the reconstruction of primitive peroxisomal proteomes suggests that ontogenetically as well as phylogenetically, peroxisomes stem from the Endoplasmic Reticulum. This article was reviewed by Arcady Mushegian, Gáspár Jékely and John Logsdon Reviewed by Arcady Mushegian, Gáspar Jékely and John Logsdon. For the full reviews, please go to the Reviewers' comments section.
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影响因子：
4.1
作者：
Abdelraheim, SR;Spiller, DG;McLennan, AG
通讯作者：
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影响因子：
3.3
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Birschmann, I;Stroobants, AK;Tabak, HF
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影响因子：
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DOI：
10.1073/pnas.0335769100
发表时间：
2003-02-04
影响因子：
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作者：
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通讯作者：
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影响因子：
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作者：
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通讯作者：
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