PEX5 Protein Binds Monomeric Catalase Blocking Its Tetramerization and Releases It upon Binding the N-terminal Domain of PEX14*
PEX5 Protein Binds Monomeric Catalase Blocking Its Tetramerization and Releases It upon Binding the N-terminal Domain of PEX14*
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PEX5 蛋白与单体过氧化氢酶结合，阻断其四聚化，并在与 PEX14* N 端结构域结合后将其释放
DOI：
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发表时间：
2011
影响因子：
4.8
通讯作者：
Jorge E Azevedo
中科院分区：
文献类型：
--
作者：
M. O. Freitas;T. Francisco;T. Rodrigues;I. Alencastre;M. P. Pinto;C. Grou;A. F. Carvalho;M. Fransen;C. Sá;Jorge E Azevedo
背景：PEX 5在细胞质中结合新合成的过氧化物酶体蛋白并将其释放到细胞器基质中。结果：PEX 5结合单体过氧化氢酶，并在PEX 14存在下释放它。结论：PEX 14参与了货物释放步骤。重要性：了解PEX 5如何与货物蛋白相互作用以及哪些因素破坏这种相互作用对于理解这种蛋白质分选途径至关重要。新合成的过氧化物酶体基质蛋白通过PEX 5靶向细胞器。PEX 5在这个过程中有双重作用。首先，它作为一种可溶性受体识别这些蛋白质在胞质溶胶。随后，在过氧化物酶体对接/易位机制中，PEX 5促进它们穿过细胞器膜的易位。尽管近年来取得了重大进展，但这一途径的几个方面仍不清楚。两个重要的是关于PEX 5-货物蛋白相互作用的形成和破坏，分别在胞质溶胶和对接/易位机制。在这里，我们提供了数据的PEX 5与过氧化氢酶，在其天然状态的同源四聚体酶的相互作用。我们发现，PEX 5与单体过氧化氢酶相互作用，产生稳定的蛋白质复合物;四聚体过氧化氢酶没有检测到这样的复合物。PEX 5与单体过氧化氢酶的结合有效地抑制其四聚化，这是一种依赖于PEX 5的N-和C-末端两半中存在的结构域的性质。有趣的是，PEX 5-过氧化氢酶相互作用被PEX 14的N-末端结构域破坏，这是对接/易位机制的一个组成部分。一个或两个的7个PEX 14结合二芳香基序中存在的N-末端一半的PEX 5可能参与这种现象。这些结果表明：1）参与与PEX 5相互作用的过氧化氢酶结构域在酶四聚化后不再可接近; 2）PEX 5中的过氧化氢酶结合界面不限于其C末端过氧化物酶体靶向序列1型结合结构域，还涉及PEX 5 N末端结构域;和3）PEX 14参与货物蛋白释放步骤。
Background: PEX5 binds newly synthesized peroxisomal proteins in the cytosol and releases them in the organelle matrix. Results: PEX5 binds monomeric catalase and releases it in the presence of PEX14. Conclusion: PEX14 participates in the cargo release step. Significance: Knowing how PEX5 interacts with cargo proteins and which factors disrupt this interaction are crucial for understanding this protein sorting pathway. Newly synthesized peroxisomal matrix proteins are targeted to the organelle by PEX5. PEX5 has a dual role in this process. First, it acts as a soluble receptor recognizing these proteins in the cytosol. Subsequently, at the peroxisomal docking/translocation machinery, PEX5 promotes their translocation across the organelle membrane. Despite significant advances made in recent years, several aspects of this pathway remain unclear. Two important ones regard the formation and disruption of the PEX5-cargo protein interaction in the cytosol and at the docking/translocation machinery, respectively. Here, we provide data on the interaction of PEX5 with catalase, a homotetrameric enzyme in its native state. We found that PEX5 interacts with monomeric catalase yielding a stable protein complex; no such complex was detected with tetrameric catalase. Binding of PEX5 to monomeric catalase potently inhibits its tetramerization, a property that depends on domains present in both the N- and C-terminal halves of PEX5. Interestingly, the PEX5-catalase interaction is disrupted by the N-terminal domain of PEX14, a component of the docking/translocation machinery. One or two of the seven PEX14-binding diaromatic motifs present in the N-terminal half of PEX5 are probably involved in this phenomenon. These results suggest the following: 1) catalase domain(s) involved in the interaction with PEX5 are no longer accessible upon tetramerization of the enzyme; 2) the catalase-binding interface in PEX5 is not restricted to its C-terminal peroxisomal targeting sequence type 1-binding domain and also involves PEX5 N-terminal domain(s); and 3) PEX14 participates in the cargo protein release step.
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影响因子：
5.6
作者：
Putnam, CD;Arvai, AS;Tainer, JA
通讯作者：
Tainer, JA
影响因子：
3.5
作者：
Braverman, N;Dodt, G;Valle, D
通讯作者：
Valle, D
影响因子：
3.3
作者：
Ma, Changle;Schumann, Uwe;Subramani, Suresh
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Subramani, Suresh
影响因子：
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作者：
MURTHY, MRN;REID, TJ;ROSSMANN, MG
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ROSSMANN, MG
乙醇氧化酶和二羟基丙酮合酶是甲基营养酵母丰富的过氧化物酶体蛋白，在不同的细胞区室中组装。
影响因子：
4
作者：
Stewart,MQ;Esposito,RD;Gowani,J;Goodman,JM
通讯作者：
Goodman,JM