N. Bies et al., Accumulation and degradation of Em proteins in Arabidopsis thaliana: Evidence for post-transcriptional controls, J EXP BOT, 49(329), 1998, pp. 1925-1933
Arabidopsis AtEm1 and AtEm6 proteins were overexpressed in E. coli and used
to raise antibodies which were used to analyse Em expression at the protei
n level. One of the sera is specific for AtEm1 protein whereas the second r
eacts with both AtEm1 and AtEm6 proteins. These antibodies were used to ana
lyse expression of Em genes at the protein level and to complete previous s
tudies at the mRNA level. During seed maturation. AtEm1 protein accumulates
earlier than AtEm6, in parallel with the corresponding mRNA but with a 3 d
delay. During germination. AtEm1 protein undergoes two successive cleavage
s before being degraded. Both proteins are much more stable than the corres
ponding mRNA. Soaking of dormant seeds indicates that imbibition is suffici
ent to induce Em protein degradation and that germination per se is not req
uired. AtEm1 and AtEm6 mRNA can be precociously induced by ABA in immature
siliques, but protein accumulation could not be observed. A similar observa
tion was made with leaves of transgenic plants ectopically expressing ABI3.
These results establish clearly that Em protein accumulation is also tight
ly controlled by post-transcriptional mechanisms in addition to transcripti
onal ones.