Abstract
Location of the proteases would affect on protease stability and photorespiratory bypass pathway, while it is unsolved. Potato rbcS signal peptide was analyzed and constructed into the protease for study of their localization site. The tartronate semialdehyde reductase (EcTSR) proteins could be accurately and efficiently located in chloroplast only when this signal peptide was extended to 80 amino acids. The signal peptide would help malate synthase (CmMS) locate to the surface of chloroplast, to form granules on the outer membrane of chloroplast. The whole spectrum scanning showed that these proteins could enter chloroplast. A signal peptide named PCS1 (Peptide of self-cleavage site 1) carrying a self-cleavage site was designed, and sixteen amino acids from the blue pigment precursor protein of chloroplast positioning signal of Silene pratensis were added to the C-terminal of PCS1. Transient expression, Western blot analysis and full-spectrum scanning showed that PCS1 could locate the EcTSR to the chloroplast, after the removal of the signal peptide.
Highlights
Photorespiration may result in a 25% loss of photosynthates in C3 plants under normal conditions, the value will be even higher if stress conditions, such as drought, heat and high light, are encountered by the plant (Peterhansel and Maurino, 2011)
Potato rbcS chloroplast positioning signal peptide was extended to 80 amino acids (StTP-80AA), GFP fluorescence crowded around the chloroplast granuli form and suggesting that the EcTSR chloroplast localization is improved (Figure 1e)
CmMS protein was fused with 58 amino acids and 80 amino acid chloroplast localization signal peptides respectively, both of them showed that these proteins were clustered around the chloroplasts (Figure 1f-g)
Summary
Photorespiration may result in a 25% loss of photosynthates in C3 plants under normal conditions, the value will be even higher if stress conditions, such as drought, heat and high light, are encountered by the plant (Peterhansel and Maurino, 2011). In 2007, bacterial glycolic acid pathways were introduced into chloroplasts to construct the first photorespiration pathway called the Kebeish pathway (Kebeish et al, 2007). Glycolate oxidase and malate synthase were located in chloroplast to build the second branch (Maier et al, 2012). By these ways, 75% of glycolic acid produced by photorespiration is transformed into the Calvin cycle. Received in revised form: 16 Mar 2020.
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