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Signal peptide peptidases are expressed in the shoot apex of rice, localized to the endoplasmic reticulum.

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Signal peptide peptidase (SPP) is a multi-transmembrane aspartic proteinase involved in regulated intramembrane proteolysis, which is implicated in fundamental life processes such as immunological response, cell signaling, tissue differentiation, and embryogenesis. In this study, we identified two

Functional diversification of thylakoidal processing peptidases in Arabidopsis thaliana.

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Thylakoidal processing peptidase (TPP) is responsible for removing amino-terminal thylakoid-transfer signals from several proteins in the thylakoid lumen. Three TPP isoforms are encoded by the nuclear genome of Arabidopsis thaliana. Previous studies showed that one of them termed plastidic type I

Nodulin 41, a novel late nodulin of common bean with peptidase activity.

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BACKGROUND The legume-rhizobium symbiosis requires the formation of root nodules, specialized organs where the nitrogen fixation process takes place. Nodule development is accompanied by the induction of specific plant genes, referred to as nodulin genes. Important roles in processes such as

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

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Type I signal peptidase (SPase I) is an integral membrane Ser/Lys protease with one or two transmembrane domains (TMDs), cleaving transport signals off translocated precursor proteins. The catalytic domain of SPase I folds to form a hydrophobic surface and inserts into the lipid bilayers at the

A novel plant enzyme with dual activity: an atypical Nudix hydrolase and a dipeptidyl peptidase III.

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In a search for plant homologues of dipeptidyl peptidase III (DPP III) family, we found a predicted protein from the moss Physcomitrella patens (UniProt entry: A9TLP4), which shared 61% sequence identity with the Arabidopsis thaliana uncharacterized protein, designated Nudix hydrolase 3. Both

Plastidic type I signal peptidase 1 is a redox-dependent thylakoidal processing peptidase.

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Thylakoids are the photosynthetic membranes in chloroplasts and cyanobacteria. The aqueous phase inside the thylakoid known as the thylakoid lumen plays an essential role in the photosynthetic electron transport. The presence and significance of thiol-disulfide exchange in this compartment have been

Dual targeting of a processing peptidase into both endosymbiotic organelles mediated by a transport signal of unusual architecture.

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As a result of the endosymbiotic gene transfer, the majority of proteins of mitochondria and chloroplasts are encoded in the nucleus and synthesized in the cytosol as precursor proteins carrying N-terminal transport signals for the 're-import' into the respective target organelle. Most of these

UBP12 and UBP13 negatively regulate the activity of the ubiquitin-dependent peptidases DA1, DAR1 and DAR2.

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Protein ubiquitination is a very diverse post-translational modification leading to protein degradation or delocalization, or altering protein activity. In Arabidopsis thaliana, two E3 ligases, BIG BROTHER (BB) and DA2, activate the latent peptidases DA1, DAR1 and DAR2 by mono-ubiquitination

Characterization of a cDNA encoding the thylakoidal processing peptidase from Arabidopsis thaliana. Implications for the origin and catalytic mechanism of the enzyme.

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We have identified and sequenced a cDNA containing a complete open reading frame for a putative 340-amino acid precursor of the thylakoidal processing peptidase from Arabidopsis thaliana. The predicted amino acid sequence of the protein includes regions highly conserved among Type I leader

Identification of cleavage sites and substrate proteins for two mitochondrial intermediate peptidases in Arabidopsis thaliana.

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Most mitochondrial proteins contain an N-terminal targeting signal that is removed by specific proteases following import. In plant mitochondria, only mitochondrial processing peptidase (MPP) has been characterized to date. Therefore, we sought to determine the substrates and cleavage sites of the

Yeast-based reporter assay system for identifying the requirements of intramembrane proteolysis by signal peptide peptidase of Arabidopsis thaliana

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Signal peptide peptidase (SPP) is an aspartic protease with two active sites, YD and GXGD in the transmembrane domain. SPP cleaves signal peptides and the released fragments play key roles in the immune system, embryo development, and protein turnover in cells. Despite SPP having an important

Signal peptide peptidase and its homologs in Arabidopsis thaliana--plant tissue-specific expression and distinct subcellular localization.

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Signal peptide peptidase (SPP) is an aspartic proteinase that hydrolyses its substrate within the plane of the cellular membrane. In vertebrates, it plays crucial roles in life processes such as differentiation, embryogenesis, cell signaling and immunological response. We first found SPP in plants.

The signal peptide peptidase is required for pollen function in Arabidopsis.

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The Signal Peptide Peptidases (SPP) are members of the Intramembrane Cleaving Proteases, which are involved in an array of protein-processing and intracellular signaling events in animals. Arabidopsis (Arabidopsis thaliana) has six genes encoding SPP-like proteins, the physiological functions of

The Plastid and Mitochondrial Peptidase Network in Arabidopsis thaliana: A Foundation for Testing Genetic Interactions and Functions in Organellar Proteostasis.

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Plant plastids and mitochondria have dynamic proteomes. Protein homeostasis in these organelles is maintained by a proteostasis network containing protein chaperones, peptidases, and their substrate recognition factors. However, many peptidases, as well as their functional connections and

Experimental detection of proteolytic activity in a signal peptide peptidase of Arabidopsis thaliana.

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BACKGROUND Signal peptide peptidase (SPP) is a multi-transmembrane aspartic protease involved in intramembrane-regulated proteolysis (RIP). RIP proteases mediate various key life events by releasing bioactive peptides from the plane of the membrane region. We have previously isolated Arabidopsis SPP

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