The Nß motif of NaTrxh directs secretion as an endoplasmic reticulum transit peptide and variations might result in different cellular targeting
Por:
Zaragoza-Gomez, Andre, Garcia-Caffarel, Emilio, Cruz-Zamora, Yuridia, Gonzalez, James, Anaya-Munoz, Victor Hugo, Cruz-Garcia, Felipe, Juarez-Diaz, Javier Andres
Publicada:
12 oct 2023
Categoría:
Multidisciplinary
Resumen:
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 N beta, 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 N beta 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
N beta 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.
Filiaciones:
Zaragoza-Gomez, Andre:
Departamento de Biología Comparada, Facultad de Ciencias, Universidad Nacional Autónoma de México, Ciudad Universitaria, UNAM, Ciudad de Mexico, Mexico
Posgrado en Ciencias Biológicas, Universidad Nacional Autónoma de México, Ciudad de Mexico, Mexico
Univ Nacl Autonoma Mexico, Fac Ciencias, Dept Biol Comparada, Ciudad Univ, Mexico City, DF, Mexico
Univ Nacl Autonoma Mexico, Posgrad Ciencias Biol, Mexico City, DF, Mexico
Garcia-Caffarel, Emilio:
Departamento de Biología Comparada, Facultad de Ciencias, Universidad Nacional Autónoma de México, Ciudad Universitaria, UNAM, Ciudad de Mexico, Mexico
Univ Nacl Autonoma Mexico, Fac Ciencias, Dept Biol Comparada, Ciudad Univ, Mexico City, DF, Mexico
Cruz-Zamora, Yuridia:
Departamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, Ciudad Universitaria, UNAM, Ciudad de Mexico, Mexico
Univ Nacl Autonoma Mexico, Dept Bioquim, Fac Quim, Ciudad Univ, Mexico City, DF, Mexico
Gonzalez, James:
Departamento de Biología Celular, Facultad de Ciencias, Universidad Nacional Autónoma de México, Ciudad Universitaria, UNAM, Ciudad de Mexico, Mexico
Univ Nacl Autonoma Mexico, Dept Biol Celular, Fac Ciencias, Ciudad Univ, Mexico City, DF, Mexico
Anaya-Munoz, Victor Hugo:
Escuela Nacional Estudios Superiores unidad Morelia, Universidad Nacional Autónoma de Mé xico, Campus Morelia, Michoacán, Morelia, Mexico
Univ Nacl Autonoma Mexico, Escuela Nacl Estudios Super Unidad Morelia, Campus Morelia, Morelia, Michoacan, Mexico
Cruz-Garcia, Felipe:
Departamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, Ciudad Universitaria, UNAM, Ciudad de Mexico, Mexico
Univ Nacl Autonoma Mexico, Dept Bioquim, Fac Quim, Ciudad Univ, Mexico City, DF, Mexico
Juarez-Diaz, Javier Andres:
Departamento de Biología Comparada, Facultad de Ciencias, Universidad Nacional Autónoma de México, Ciudad Universitaria, UNAM, Ciudad de Mexico, Mexico
Univ Nacl Autonoma Mexico, Fac Ciencias, Dept Biol Comparada, Ciudad Univ, Mexico City, DF, Mexico
gold, All Open Access; Gold
|