M. Heinlein et al., IN-VIVO AGGREGATION OF MAIZE ACTIVATOR (AC) TRANSPOSASE IN NUCLEI OF MAIZE ENDOSPERM AND PETUNIA PROTOPLASTS, Plant journal, 5(5), 1994, pp. 705-714
The transposase (TPase) of the maize transposon Activator (Ac) accumul
ates in the nuclei of maize endosperm and transfected Petunia protopla
sts, where it aggregates into rod-like structures about 2 mu m in leng
th. In petunia protoplasts the amount of TPase aggregates increases wi
th the strength of the promoter fused to the Ac-coding region. The exc
ision frequency of a Ds element, however, does not increase proportion
ally. The data suggest that the aggregated TPase is not responsible fo
r the mobilization of the Ds element, but rather is a transpositionall
y inactive form of the protein. In contrast to the full-length TPase,
a functional, N-terminally truncated TPase derivative is inefficiently
transported into the nucleus at high expression levels and aggregates
predominantly in the cytoplasm. Accordingly, the N-terminus of the TP
ase is involved in nuclear localization and/or aggregation.