The chloroplast localization of protease mediated by the potato rbcS signal peptide and its improvement for construction of photorespiratory bypasses

  • Zhen YAO Yangtze University, College of Horticulture and Gardening, Jingzhou, 434025 https://orcid.org/0000-0002-1750-5203
  • Boran SHEN South China Agricultural University, Laboratory of Molecular Plant Physiology, College of Life Sciences, Guangzhou, 510640
  • Xiulan YANG Yangtze University, Department of Medicine, Jingzhou, 434025
  • Minhui LONG South China Normal University, College of Life science, Guangzhou, 510631
Keywords: chloroplast localization; chloroplast signal peptide; photorespiratory bypass

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.

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Published
2020-03-31
How to Cite
YAO, Z., SHEN, B., YANG, X., & LONG, M. (2020). The chloroplast localization of protease mediated by the potato rbcS signal peptide and its improvement for construction of photorespiratory bypasses. Notulae Botanicae Horti Agrobotanici Cluj-Napoca, 48(1), 14-23. https://doi.org/10.15835/nbha48111762
Section
Research Articles