Stable complex formation of thylakoidal processing peptidase and PGRL1
Copyright policy )Stable complex formation of thylakoidal processing peptidase and PGRL1
The thylakoid‐transfer signal is required for energy‐dependent translocation of preproteins into the thylakoid lumen and is removed by the thylakoidal processing peptidase (TPP). PGRL1 is an essential component of antimycin A‐sensitive photosynthetic cyclic electron flow in chloroplasts. Here we report that one of the TPP isoforms, Plsp1, forms a stable complex with PGRL1. Genetic data demonstrate that PGRL1 is not essential for Plsp1 activity in vivo, leading to a possibility that PGRL1 may act as a regulator of TPP.
- University of California, Davis United States
PGRL1, Plastidic type I signal peptidase1 (Plsp1), Arabidopsis Proteins, Serine Endopeptidases, Arabidopsis, Membrane Proteins, Chloroplast, Thylakoids, Membrane protein complex, Seedlings, Multiprotein Complexes, Enzyme Stability, Thylakoid, Genes, Lethal, Protein Multimerization, Blue native-polyacrylamide gel electrophoresis
PGRL1, Plastidic type I signal peptidase1 (Plsp1), Arabidopsis Proteins, Serine Endopeptidases, Arabidopsis, Membrane Proteins, Chloroplast, Thylakoids, Membrane protein complex, Seedlings, Multiprotein Complexes, Enzyme Stability, Thylakoid, Genes, Lethal, Protein Multimerization, Blue native-polyacrylamide gel electrophoresis
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