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单一过氧化物酶体靶向信号介导硅藻基质蛋白的输入。

A single peroxisomal targeting signal mediates matrix protein import in diatoms.

机构信息

Laboratory for Cell Biology, Philipps University of Marburg, Marburg, Germany.

出版信息

PLoS One. 2011;6(9):e25316. doi: 10.1371/journal.pone.0025316. Epub 2011 Sep 22.

Abstract

Peroxisomes are single membrane bound compartments. They are thought to be present in almost all eukaryotic cells, although the bulk of our knowledge about peroxisomes has been generated from only a handful of model organisms. Peroxisomal matrix proteins are synthesized cytosolically and posttranslationally imported into the peroxisomal matrix. The import is generally thought to be mediated by two different targeting signals. These are respectively recognized by the two import receptor proteins Pex5 and Pex7, which facilitate transport across the peroxisomal membrane. Here, we show the first in vivo localization studies of peroxisomes in a representative organism of the ecologically relevant group of diatoms using fluorescence and transmission electron microscopy. By expression of various homologous and heterologous fusion proteins we demonstrate that targeting of Phaeodactylum tricornutum peroxisomal matrix proteins is mediated only by PTS1 targeting signals, also for proteins that are in other systems imported via a PTS2 mode of action. Additional in silico analyses suggest this surprising finding may also apply to further diatoms. Our data suggest that loss of the PTS2 peroxisomal import signal is not reserved to Caenorhabditis elegans as a single exception, but has also occurred in evolutionary divergent organisms. Obviously, targeting switching from PTS2 to PTS1 across different major eukaryotic groups might have occurred for different reasons. Thus, our findings question the widespread assumption that import of peroxisomal matrix proteins is generally mediated by two different targeting signals. Our results implicate that there apparently must have been an event causing the loss of one targeting signal even in the group of diatoms. Different possibilities are discussed that indicate multiple reasons for the detected targeting switching from PTS2 to PTS1.

摘要

过氧化物酶体是单层膜结合的隔室。它们被认为存在于几乎所有真核细胞中,尽管我们对过氧化物酶体的大部分了解都是从少数几种模式生物中获得的。过氧化物酶体基质蛋白在细胞质中合成,并在翻译后被导入过氧化物酶体基质中。一般认为,这种导入是由两种不同的靶向信号介导的。这两种信号分别被两种不同的输入受体蛋白 Pex5 和 Pex7 识别,它们促进了过氧化物酶体膜的运输。在这里,我们使用荧光和透射电子显微镜,对生态相关的硅藻组的一个代表性生物进行了首次过氧化物酶体的体内定位研究。通过表达各种同源和异源融合蛋白,我们证明 Phaeodactylum tricornutum 过氧化物酶体基质蛋白的靶向仅由 PTS1 靶向信号介导,对于通过 PTS2 作用模式导入的蛋白质也是如此。进一步的计算机分析表明,这一令人惊讶的发现可能也适用于其他硅藻。我们的数据表明,PTS2 过氧化物酶体输入信号的丢失并不是线虫这一个体作为单一例外而保留的,而是在进化上不同的生物中也发生了。显然,不同主要真核生物群体之间从 PTS2 到 PTS1 的靶向转换可能是由于不同的原因。因此,我们的发现质疑了过氧化物酶体基质蛋白的导入通常是由两种不同的靶向信号介导的广泛假设。我们的结果表明,显然在硅藻群体中,即使在一个群体中,也发生了导致一个靶向信号丢失的事件。讨论了不同的可能性,表明从 PTS2 到 PTS1 的靶向转换可能有多种原因。

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