Disordered plant chaperones play key roles in helping plants survive in harsh conditions,
and they are indispensable for seeds to remain viable. Aside from well-known and thoroughly
characterized globular chaperone proteins, there are a number of intrinsically disordered
proteins (IDPs) that can also serve as highly effective protecting agents in the cells.
One of the largest groups of disordered chaperones is the group of dehydrins, proteins
that are expressed at high levels under different abiotic stress conditions, such
as drought, high temperature, or osmotic stress. Dehydrins are characterized by the
presence of different conserved sequence motifs that also serve as the basis for their
categorization. Despite their accepted importance, the exact role and relevance of
the conserved regions have not yet been formally addressed. Here, we explored the
involvement of each conserved segment in the protective function of the intrinsically
disordered stress protein (IDSP) A. thaliana’s Early Response to Dehydration (ERD14).
We show that segments that are directly involved in partner binding, and others that
are not, are equally necessary for proper function and that cellular protection emerges
from the balanced interplay of different regions of ERD14.
