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

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

PROVIDER: PRJNA530177 | ENA |

REPOSITORIES: ENA

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

Project description: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.

2019-09-01 | GSE129113 | GEO

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.

2021-07-05 | PXD022002 | Pride

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

Project description:iRhoms are pseudoprotease members of the rhomboid-like superfamily and are cardinal regulators of inflammatory and growth factor signaling; they function primarily by recognizing transmembrane domains of their clients. Here, we report a mechanistically distinct nuclear function of iRhoms, showing that both human and mouse iRhom2 are non-canonical substrates of signal peptidase complex (SPC), the protease that removes signal peptides from secreted proteins. Cleavage of iRhom2 generates an N-terminal fragment that enters the nucleus and modifies the transcriptome, in part by binding C-terminal binding proteins (CtBPs). The biological significance of nuclear iRhom2 is indicated by elevated levels in skin biopsies of patients with psoriasis, tylosis with oesophageal cancer (TOC), and non-epidermolytic palmoplantar keratoderma (NEPPK); increased iRhom2 cleavage in a keratinocyte model of psoriasis; and nuclear iRhom2 promoting proliferation of keratinocytes. Overall, this work identifies an unexpected SPC-dependent ER-to-nucleus signaling pathway and demonstrates that iRhoms can mediate nuclear signaling.

2024-01-04 | GSE219008 | GEO

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

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Dipeptidyl peptidase-IV is associated with decreased glioma growth

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Vigilin interacts with signal peptide peptidase.

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Three-dimensional structure of the signal peptide peptidase.

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Veterinary trypanocidal benzoxaboroles are peptidase-activated prodrugs

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Modeling Escherichia coli signal peptidase complex with bound substrate: determinants in the mature peptide influencing signal peptide cleavage.

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