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Comparative analysis of gene expression between overexpression and deficiency of signal peptide peptidase in Arabidopsis thaliana

ABSTRACT: Signal peptide peptidase (SPP) plays an essential role in among all eukaryotes. The knock out lines of A. thaliana SPP (AtSPP) is lethal and the substrates of AtSPP are not identified. Based on the situation, we constructed the plants with AtSPP over-expressed and knock down to investigate the role of AtSPP. We also used the data to find the candidate substrates of AtSPP, which regulates intermembrane proteolysis, would have crucial physiological functions as well as control the gene expression encoding the substrates.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE129113 | GEO | 2019/09/01

REPOSITORIES: GEO

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Cleavage of the pseudoprotease iRhom2 by the signal peptidase complex reveals an ER-to-nucleus signalling pathway

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Bunyamwera orthobunyavirus glycoprotein precursor is processed by cellular signal peptidase and signal peptide peptidase.

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Structure of the human signal peptidase complex

Project description:The ER-resident signal peptidase complex (SPC) is an essential membrane protein complex involved in the maturation of soluble and type-I transmembrane proteins destined to the secretory pathway. As a part of the ER translocon machinery, the SPC removes signal peptides (SPs) from the N-termini of many proteins such as hormones, antibodies, or secretory enzymes1,2. To accomplish this task, the SPC must process a large variety of SPs with an exquisite specificity. Although the determinants of SP recognition have been established empirically3, the molecular details of SP recognition and removal remain elusive. Here, we show that the human SPC exists in two functional paralogs with distinct proteolytic subunits. We determined the structures and posttranslational modifications of both paralogs using electron cryo-microscopy and structural proteomics. The respective proteolytic subunits SEC11A and SEC11C adopt a conserved signal peptidase (SPase) fold with their active sites facing a prominent transmembrane window, which is collectively formed by the transmembrane domains of all SPC subunits. Characteristic, charged regions on both sides of this window locally thin the membrane by approximately 40% compared to the exterior. The data suggest a mechanistic model for SPC specificity and the transfer of SPs from the Sec61 translocation channel to the SPC.

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Comparative analysis of gene expression between overexpression and deficiency of signal peptide peptidase in Arabidopsis thaliana

Project description:Comparative analysis of gene expression between overexpression and deficiency of signal peptide peptidase in Arabidopsis thaliana

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Project description:Signal peptide peptidase (SPP) is an atypical aspartic protease that hydrolyzes peptide bonds within the transmembrane domain of substrates and is implicated in several biological and pathological functions. Here, we analyzed the structure of human SPP by electron microscopy and reconstructed the three-dimensional structure at a resolution of 22 Å. Enzymatically active SPP forms a slender, bullet-shaped homotetramer with dimensions of 85 × 85 × 130 Å. The SPP complex has four concaves on the rhombus-like sides, connected to a large chamber inside the molecule. Intriguingly, the N-terminal region of SPP is sufficient for the tetrameric assembly. Moreover, overexpression of the N-terminal region inhibited the formation of the endogenous SPP tetramer and the proteolytic activity within cells. These data suggest that the homotetramer is the functional unit of SPP and that its N-terminal region, which works as the structural scaffold, has a novel modulatory function for the intramembrane-cleaving activity of SPP.

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