Agriculture Reference
In-Depth Information
Figure 7. The growth patterns of the wild-type and the
R3-1
mutant in planter after
treatment of germinating seeds to expose at 35
℃
under light for 7 days.
The mutant molecule of transit peptide-NDPK2 Ile12Leu Glu205Lys will
result in faster phosphorylation and subsequent phospho relay to high
molecular weight histidine kinases will occur rapidly in the
R3-1
, as shown in
Figure 2a. Such a situation will permit the earlier response of hook opening
and the faster leaf opening in the
R3-1
mutant than those in the wild-type.
Large amount of transit peptide-NDPK2 in wild-type and transit peptide-
NDPK2 Ile12Leu Glu205Lys in the mutant
R3-1
forming complex with
catalases in the cytosol will function to supply electron to the singlet oxygen
forming a superoxide. The amount of superoxide supplied via the protein
complexes will be larger in the
R3-1
mutant, because the rate of
autophosphorylation activity of the transit peptide-NDPK2 Ile12Leu
Glu205Lys was larger than that in the wild-type. The amount of superoxide
supplyed in the cytosol in the
R3-1
will be larger than that in the wild-type,
which will easily be detoxified to H
2
O
2
and further to H
2
O +
3
O
2
+ thermal
emission. This situation will confer the
R3-1
mutant to show 2-fold increase in
the yield of pods and total plant weights compared with wild-type did.
High temperature resistant phenotype of the
R3-1
mutant will be the result
of high activity of transit peptide-NDPK2 Ile12Leu Glu205Lys in the
R3-1
. In
Saccharum officinarum
heat shock of the cultured cells showed enhanced
phosphorylation of NDPK (Moisyadi et al., 1994). Further enhanced
phosphorylation of the transit peptide-NDPK2 Ile12Leu Glu205Lys in the
R3-
1
will phosphorylate high molecular weight histidine kinases by phospho relay
(Hasunuma et al., 2012). The function of these high molecular weight histidine
kinases was not yet known. However, most of stress responses showed relation
to high molecular weight histidine kinases, which will be estimated to have a
