Περίληψη:
Plant natriuretic peptides (PNPs) are hormones that have been extracted
from many different species, with the Arabidopsis thaliana PNP (AtPNP-A)
being the most studied among them. AtPNP-A is a signaling molecule that
consists of 130 residues and is secreted into the apoplast, under
conditions of biotic or abiotic stress. AtPNP-A has distant sequence
homology with human ANP, a protein that forms amyloid fibrils in vivo.
In this work, we investigated the amyloidogenic properties of a
34-residue-long peptide, located within the AtPNP-A sequence, in three
different pH conditions, using transmission electron microscopy, X-ray
fiber diffraction, ATR FT-IR spectroscopy, Congo red and Thioflavin T
staining assays. We also utilize bioinformatics tools to study its
association with known plant amyloidogenic proteins and other A.
thaliana proteins. Our results reveal a new case of a pH-dependent
amyloid forming peptide in A. thaliana, with a potential functional
role.
Συγγραφείς:
Nasi, Georgia I.
Aktypi, Foteini D.
Spatharas, Panagiotis M. and
Louros, Nikolaos N.
Tsiolaki, Paraskevi L.
Magafa, Vassiliki and
Trougakos, Ioannis P.
Iconomidou, Vassiliki A.
