A. Kalinski et al., THE EXPRESSION AND ACCUMULATION OF SOYBEAN VEGETATIVE-CELL THIOL PROTEASE IS TEMPORALLY AND DEVELOPMENTALLY-REGULATED, Plant physiology and biochemistry, 35(10), 1997, pp. 795-802
Plants possess a salvage pathway in which proteins accumulated during
prior developmental stages are catabolized and recycled as building bl
ocks for new rounds of synthesis. Soybean leaves and pods accumulate v
egetative storage proteins prior to and during reproductive stage that
function as transient nitrogen resources. These proteins are mobilize
d to provide carbon and nitrogen for the synthesis of seed storage pro
teins during seed maturation. We have isolated two thiol protease cDNA
s that correspond to the two isoforms that are expressed in, soybean l
eaves and pods. Immunoblot analysis with an antipeptide antibody elici
ted against the 15 C-terminal amino acids of the leaf protease cross-r
eact with an identical Mr polypeptide in leaves, pods, roots, flowers
and cotyledons after 9 days of seedling growth. The distribution of th
e protease in various soybean organs indicates the thiol protease is a
vegetative cell protease. The expression of the vegetative protease m
RNA in soybean leaves occurs during leaf expansion but only after the
leaves are sufficiently mature to undergo the sink to source transitio
n. In contrast thiol protease gene expression in pods occurs throughou
t seed maturation. The leaves of podded and depodded soybean plants bo
th express the thiol protease mRNAs, however depodding soybean plants
partially represses thiol protease gene expression. The expression of
the leaf protease is subject to temporal control with higher levels of
expression occuring in the late afternoon in plants exposed to the am
bient day/night cycle. The accumulation of the proteins encoded by the
vegetative thiol protease mRNAs are likely to be responsible for amin
o acid salvage from vegetative storage protein.