The Nβ motif of NaTrxh directs secretion as an endoplasmic reticulum transit peptide and variations might result in different cellular targeting

Soluble secretory proteins with a signal peptide reach the extracellular space through the endoplasmic reticulum-Golgi conventional pathway. During translation, the signal peptide is recognised by the signal recognition particle and results in a co-translational translocation to the endoplasmic reti...

Full description

Saved in:
Bibliographic Details
Published in:PloS one 2023-10, Vol.18 (10), p.e0287087-e0287087
Main Authors: Zaragoza-Gómez, Andre, García-Caffarel, Emilio, Cruz-Zamora, Yuridia, González, James, Anaya-Muñoz, Víctor Hugo, Cruz-García, Felipe, Juárez-Díaz, Javier Andrés
Format: Article
Language:English
Subjects:
Amino acids
Biology and Life Sciences
C-Terminus
Cell division
Endoplasmic reticulum
Golgi apparatus
Localization
Peptides
Post-translation
Proteins
Research and Analysis Methods
Residues
Secretion
Signal recognition particle
Thioredoxin
Translation
Translocation
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Soluble secretory proteins with a signal peptide reach the extracellular space through the endoplasmic reticulum-Golgi conventional pathway. During translation, the signal peptide is recognised by the signal recognition particle and results in a co-translational translocation to the endoplasmic reticulum to continue the secretory pathway. However, soluble secretory proteins lacking a signal peptide are also abundant, and several unconventional (endoplasmic reticulum/Golgi independent) pathways have been proposed and some demonstrated. This work describes new features of the secretion signal called Nβ, originally identified in NaTrxh, a plant extracellular thioredoxin, that does not possess an orthodox signal peptide. We provide evidence that other proteins, including thioredoxins type h , with similar sequences are also signal peptide-lacking secretory proteins. To be a secretion signal, positions 5, 8 and 9 must contain neutral residues in plant proteins–a negative residue in position 8 is suggested in animal proteins–to maintain the Nβ motif negatively charged and a hydrophilic profile. Moreover, our results suggest that the NaTrxh translocation to the endoplasmic reticulum occurs as a post-translational event. Finally, the Nβ motif sequence at the N- or C-terminus could be a feature that may help to predict protein localisation, mainly in plant and animal proteins.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0287087