Direct protein delivery into intact plant cells using polyhistidine peptides

Author:

Tanaka Yoshino1,Nanasato Yoshihiko2,Omura Kousei1,Endoh Keita3,Kawano Tsuyoshi1,Iwasaki Takashi1ORCID

Affiliation:

1. Department of Agriculture, Graduate School of Sustainability Science, Tottori University, Tottori, Japan

2. Forest Bio-Research Center, Forestry and Forest Products Research Institute, Hitachi, Ibaraki, Japan

3. Forest Tree Breeding Center, Forestry and Forest Products Research Institute, Hitachi, Ibaraki, Japan

Abstract

ABSTRACT Polyhistidine peptides (PHPs), sequences comprising only histidine residues (>His8), are effective cell-penetrating peptides for plant cells. Using PHP-fusion proteins, we aimed to deliver proteins into cultured plant cells from Nicotiana tabacum, Oryza sativa, and Cryptomeria japonica. Co-cultivation of cultured cells with fusion proteins combining maltose-binding protein (MBP), red fluorescent protein (RFP), and various PHPs (MBP–RFP–His8–His20) in one polypeptide showed the cellular uptake of fusion proteins in all plant cell lines. Maximum intracellular fluorescence was shown in MBP-RFP-His20. Further, adenylate cyclase (CyaA), a synthase of cyclic adenosine monophosphate (cAMP) activated by cytosolic calmodulin, was used as a reporter for protein delivery in living cells. A fusion protein combining MBP, RFP, CyaA, and His20 (MBP–RFP–CyaA–His20) was delivered into plant cells and increased intracellular fluorescence and cAMP production in all cell lines. The present study demonstrates that PHPs are effective carriers of proteins into the intracellular space of various cultured plant cells.

Funder

Japan Society for the Promotion of Science

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

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