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Proceedings of the National Academy of Sciences, Vol 88, 9984-9988, Copyright © 1991 by National Academy of Sciences
J Zeng, BL Vallee and JHR Kagi
The rapid induction of thionein (apometallothionein) by many endogenous
stimuli such as steroid hormones, cytokines, and second messengers suggests
that this cysteine-rich, metal binding protein participates in an as yet
undefined role in cellular regulatory processes. This study demonstrates
with DNA and RNA binding assays and in vitro transcription measurements
that thionein suppresses the binding of the Xenopus laevis zinc finger
transcription factor IIIA (TFIIIA) to 5S RNA and to the 5S RNA gene and
abrogates the capacity of TFIIIA to initiate the RNA polymerase
III-catalyzed synthesis of 5S RNA. The effect is reversed by the addition
of zinc and is not observed in the TFIIIA-independent transcription of a
tRNA gene by the same RNA polymerase. In view of the strong tendency of
thionein to complex posttransition metals such as zinc, one effect of its
enhanced synthesis in vivo could be to reduce the intracellular
disposability of zinc and thus modulate the actions of zinc-dependent
enzymes and proteins, most notably those of the zinc finger transcription
factors.
ARTICLE
Zinc Transfer from Transcription Factor IIIA Fingers to Thionein Clusters
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