The ten amino acids of the oxygen-evolving enhancer of tobacco is sufficient as the peptide residues for protein transport to the chloroplast thylakoid.

Content Provider	Europe PMC
Author	Ma, Sang Hoon Kim, Hyun Min Park, Se Hee Park, Seo Young Mai, Thanh Dat Do, Ju Hui Koo, Yeonjong Joung, Young Hee
Abstract	Key messageThe thylakoid transit peptide of tobacco oxygen-evolving enhancer protein contains a minimal ten amino acid sequences for thylakoid lumen transports. This ten amino acids do not contain twin-arginine, which is required for typical chloroplast lumen translocation.AbstractChloroplasts are intracellular organelles responsible for photosynthesis to produce organic carbon for all organisms. Numerous proteins must be transported from the cytosol to chloroplasts to support photosynthesis. This transport is facilitated by chloroplast transit peptides (TPs). Four chloroplast thylakoid lumen TPs were isolated from Nicotiana tabacum and were functionally analyzed as thylakoid lumen TPs. Typical chloroplast stroma-transit peptides and thylakoid lumen transit peptides (tTPs) are found in N. tabacum transit peptides (NtTPs) and the functions of these peptides are confirmed with TP–GFP fusion proteins under fluorescence microscopy and chloroplast fractionation, followed by Western blot analysis. During the functional analysis of tTPs, we uncovered the minimum 10 amino acid sequence is sufficient for thylakoid lumen transport. These ten amino acids can efficiently translocate GFP protein, even if they do not contain the twin-arginine residues required for the twin-arginine translocation (Tat) pathway, which is a typical thylakoid lumen transport. Further, thylakoid lumen transporting processes through the Tat pathway was examined by analyzing tTP sequence functions and we demonstrate that the importance of hydrophobic core for the tTP cleavage and target protein translocation.Supplementary InformationThe online version of this article (10.1007/s11103-020-01106-8) contains supplementary material, which is available to authorized users.
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ISSN	01674412
Journal	Plant Molecular Biology [Plant Mol Biol]
Volume Number	105
DOI	10.1007/s11103-020-01106-8
PubMed Central reference number	PMC7892526
Issue Number	4
Issue Number	4-5
PubMed reference number	33393067
e-ISSN	15735028
Language	English
Publisher	Springer Netherlands
Publisher Date	2021-01-03
Publisher Place	Dordrecht
Access Restriction	Open
Rights License	Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. © The Author(s) 2021, corrected publication 2021
Subject Keyword	Chloroplast Tat pathway Thylakoid lumen Transit peptides
Content Type	Text
Resource Type	Article
Subject	Genetics Plant Science Medicine Agronomy and Crop Science