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Recognition of a signal peptide by the signal recognition particle

机译：信号识别颗粒对信号肽的识别

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摘要

Targeting of proteins to appropriate subcellular compartments is a crucial process in all living cells. Secretory and membrane proteins usually contain an amino-terminal signal peptide, which is recognized by the signal recognition particle (SRP) when nascent polypeptide chains emerge from the ribosome. The SRP-ribosome nascent chain complex is then targeted through its GTP-dependent interaction with SRP receptor to the protein-conducting channel on endoplasmic reticulum membrane in eukaryotes or plasma membrane in bacteria. A universally conserved component of SRP (refs 1, 2), SRP54 or its bacterial homo-logue, fifty-four homologue (Ffh), binds the signal peptides, which have a highly divergent sequence divisible into a positively charged n-region, an h-region commonly containing 8-20 hydrophobic residues and a polar c-region. No structure has been reported that exemplifies SRP54 binding of any signal sequence. Here we have produced a fusion protein between Sulfolobus solfataricus SRP54 (Ffh) and a signal peptide connected via a flexible linker. This fusion protein oligomerizes in solution through interaction between the SRP54 and signal peptide moieties belonging to different chains, and it is functional, as demonstrated by its ability to bind SRP RNA and SRP receptor FtsY. We present the crystal structure at 3.5 A resolution of an SRP54-signal peptide complex in the dimer, which reveals how a signal sequence is recognized by SRP54.
机译：在所有活细胞中，将蛋白质靶向适当的亚细胞区室是至关重要的过程。分泌蛋白和膜蛋白通常包含一个氨基末端信号肽，当新生的多肽链从核糖体中出来时，该信号肽会被信号识别颗粒（SRP）识别。然后，通过SRP核糖体新生链复合物通过与SRP受体的GTP依赖性相互作用，靶向真核生物内质网膜或细菌质膜上的蛋白质传导通道。 SRP的通用保守成分（参考文献1、2），SRP54或它的细菌同源物54同源物（Ffh）与信号肽结合，该信号肽具有高度分歧的序列，可分为带正电荷的n区，即h区通常包含8-20个疏水残基和一个极性c区。没有报道可例示任何信号序列与SRP54结合的结构。在这里，我们生产了Sulfolobus solfataricus SRP54（Ffh）和通过柔性接头连接的信号肽之间的融合蛋白。该融合蛋白通过SRP54与属于不同链的信号肽部分之间的相互作用在溶液中寡聚，并且具有功能性，如其结合SRP RNA和SRP受体FtsY的能力所证明。我们在二聚体中以SRP54-信号肽复合物的3.5 A分辨率显示晶体结构，这揭示了SRP54如何识别信号序列。

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  • 来源
    《Nature》 |2010年第7297期|p.507-510|共4页
  • 作者

    Claudia Y. Janda; Jade Li; Chris Oubridge; Helena Hernandez; Carol V. Robinson; Kiyoshi Nagai;

  • 作者单位

    MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK Department of Molecular and Cellular Physiology and Department of Structural Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305, USA;

    MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK;

    MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK;

    University of Cambridge Chemical Laboratories, Lensfield Road, Cambridge CB2 1EW, UK Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK;

    University of Cambridge Chemical Laboratories, Lensfield Road, Cambridge CB2 1EW, UK Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK;

    MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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