Plants respond to stress conditions through
early stress-response factors (ESRF), which serve the
function of stress sensing and/or signal transduction. These
mainly comprise qualitative and/or quantitative flux in the
redox molecules, calcium ions (Ca2?), phosphatidic acid,
hexose sugars and phytohormones. The role of resident
proteins such as phytohormone receptors and G-proteins as
first messengers under stress is well established. Yet,
within the modern omics context, most of the stress
response at the protein level is injudiciously attributed to
substantial up- or down-regulation of expression measured
at the RNA or protein level. Proteins such as kinases and
transcription factors (TFs) that exhibit cascade effects are
primary candidates for studies in plant stress tolerance.
However, resident-protein post-translational modification
(PTM), specifically in response to particular conditions
such as stress, is a candidate for immediate and potent
‘quick reaction force’ (QRF) kind of effects. Stress-mediated
SUMOylation of TFs and other proteins have been
observed. SUMOylation can change the rate of activity,
function or location of the modified protein. Early SUMOylation
of resident proteins can act in the stress signal
transduction or in adaptive response. Here, we consider
brief background information on ESRFs to establish the
crosstalk between these factors that impinge on PTMs. Wethen illustrate connections of protein SUMOylation to
phytohormones and TFs. Finally, we present results of an
in silico analysis of rice Receptor-Like Kinases, heat-shock
and calcium-binding proteins to identify members of these
gene families, whose basal expression under drought but
potential SUMOylation presents them as QRF candidates
for roles in stress signaling/response.