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Literature summary for 3.4.21.89 extracted from

  • Endow, J.K.; Singhal, R.; Fernandez, D.E.; Inoue, K.
    Chaperone-assisted post-translational transport of plastidic type I signal peptidase 1 (2015), J. Biol. Chem., 290, 28778-28791 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information using a heterologous system, targeting of Arabidopsis thaliana Plsp1 to pea chloroplasts/chloroplast membranes is performed Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast stroma Plsp1 accumulates as a stromal intermediate before ATP hydrolysis-dependent membrane association Arabidopsis thaliana 9570
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membrane the enzyme is a transmembrane protein. Plsp1 accumulates as a stromal intermediate before ATP hydrolysis-dependent membrane association Arabidopsis thaliana 16020
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additional information two distinct stromal components are involved in post-translational transport of plastidic SPase I 1 (Plsp1) from Arabidopsis thaliana, which contains a single transmembrane domain. During import into isolated chloroplasts, Plsp1 is targeted to the membrane via a soluble intermediate in an ATP hydrolysis-dependent manner. Insertion of Plsp1 into isolated chloroplast membranes, by contrast, is found to occur by two distinct mechanisms. The first mechanism requires ATP hydrolysis and the protein conducting channel cpSecY1 and is strongly enhanced by exogenously added cpSecA1. The second mechanism is independent of nucleoside triphosphates and proteinaceous components but with a high frequency of mis-orientation. This unassisted insertion is inhibited by urea and stroma extract. During import-chase assays using intact chloroplasts, Plsp1 is incorporated into a soluble 700-kDa complex that co-migrates with the Cpn60 complex before inserting into the membrane. The transmembrane domain within Plsp1 is required for the cpSecA1-dependent insertion but is dispensable for association with the 700-kDa complex and also for unassisted membrane insertion. Cooperation of Cpn60 and cpSecA1 for proper membrane insertion of Plsp1 by cpSecY1. Mechanism of Plsp1 transport, overview. The lumenal portion of Plsp1 can spontaneously insert into the membrane from the cis-side, but this nonspecific event is prevented by integration into a large complex in the stroma that co-migrates with a chaperonin-60 (Cpn60) complex. Import of the Arabidopsis enzyme into isolated pea chloroplasts. The C-terminal portion of Plsp1 including catalytic residues is predicted to form a hydrophobic surface at the trans-side of the membrane. This folding is necessary for hydrolysis of peptide bonds near or in the membrane at the trans-side, although premature folding would lead to incorrect insertion from the cis-side Arabidopsis thaliana
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thylakoid membrane
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 Arabidopsis thaliana 42651
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Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q8H0W1
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Posttranslational Modification

Posttranslational Modification Comment Organism
additional information chaperone-assisted post-translational transport of plastidic type I signal peptidase 1, mechanism of Plsp1 transport, overview Arabidopsis thaliana
proteolytic modification enzyme Plsp1 is encoded as a larger precursor (prPlsp1) in the nuclear genome, prPlsp1 carries an N-terminal extension. This transit peptide the N-terminal extension of Plsp1 is necessary for import and also sufficient for targeting a passenger protein, citrine, to the chloroplast stroma. It is cleaved after residue 67 Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining
leaf
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 Arabidopsis thaliana
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Synonyms

Synonyms Comment Organism
chloroplast processing peptidase
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 Arabidopsis thaliana
plastidic SPase I 1
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 Arabidopsis thaliana
Plsp1
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 Arabidopsis thaliana
signal peptidase I-3
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 Arabidopsis thaliana
SPase I 1
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 Arabidopsis thaliana
type I signal peptidase 1
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 Arabidopsis thaliana

General Information

General Information Comment Organism
evolution evolutionary adaptation from the ribosome-dependent co-translational insertion to the chaperone-dependent post-translational transport of SPase I Arabidopsis thaliana
additional information the energy requirement of integration of Plsp1 into isolated chloroplast membranes are satified by ATP hydrolysis. The C-terminal portion of Plsp1 including catalytic residues is predicted to form a hydrophobic surface at the trans-side of the membrane Arabidopsis thaliana