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Plant Physiol, April 2000, Vol. 122, pp. 1355-1364
Calcium-Independent Activation of Salicylic Acid-Induced Protein
Kinase and a 40-Kilodalton Protein Kinase by Hyperosmotic
Stress1
Mary Elizabeth
Hoyos and
Shuqun
Zhang*
Department of Biochemistry, University of Missouri-Columbia, 117 Schweitzer Hall, Columbia, Missouri 65211
Reversible protein
phosphorylation/dephosphorylation plays important roles in signaling
the plant adaptive responses to salinity/drought stresses. Two protein
kinases with molecular masses of 48 and 40 kD are activated in tobacco
cells exposed to NaCl. The 48-kD protein kinase was identified as SIPK
(salicylic acid-induced protein kinase), a member of the tobacco MAPK
(mitogen-activated protein kinase) family that is activated by various
other stress stimuli. The activation of the 40-kD protein kinase is
rapid and dose-dependent. Other osmolytes such as Pro and sorbitol
activate these two kinases with similar kinetics. The activation of
40-kD protein kinase is specific for hyperosmotic stress, as hypotonic stress does not activate it. Therefore, this 40-kD kinase
was named HOSAK (high osmotic stress-activated kinase). HOSAK is a Ca2+-independent kinase and uses myelin basic protein (MBP)
and histone equally well as substrates. The kinase inhibitor K252a
rapidly activates HOSAK in tobacco cells, implicating a
dephosphorylation mechanism for HOSAK activation. Activation of both
SIPK and HOSAK by high osmotic stress is Ca2+ and abscisic
acid (ABA) independent. Furthermore, mutation in SOS3
locus does not affect the activation of either kinase in Arabidopsis
seedlings. These results suggest that SIPK and 40-kD HOSAK are two new
components in a Ca2+- and ABA-independent pathway that may
lead to plant adaptation to hyperosmotic stress.
1
This work was supported by a grant from the
University of Missouri Research Board (to S.Z.).
*
Corresponding author; e-mail zhangsh{at}missouri.edu; fax
573-884-4812.
© 2000 American Society of Plant Physiologists
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