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Following protein synthesis inhibition in cycloheximide
growth-arrested yeast cells, the rates of tRNA and 5 S RNA synthesis
decrease with apparent half-times of about 20 and 10 min, respectively.
This effect is mimicked by extracts of treated cells, and the
impairment of tRNA gene transcription activity that is observed in
vitro parallels the in vivo inactivation of RNA
polymerase III transcription. As revealed by experiments in which
partially purified class III transcription factors were singly added to
extracts of treated cells, only the activity of the multiprotein
transcription factor TFIIIB is severely impaired after 3 h of
cycloheximide treatment. Similar assays carried out in an in vitro transcription system in which TFIIIB activity was reconstituted by
a combination of the TATA box-binding protein (TBP), the 70-kDa
component TFIIIB70, plus a partially purified fraction known as B" have
shown that the latter two components are both necessary and sufficient
to restore control levels of transcription. Their activity, but not TBP
activity, is considerably reduced in extracts of treated cells.
TFIIIB70 and a component of fraction B" thus appear to be the selective
targets of the down-regulation of polymerase III transcription that is
brought about by cycloheximide. A substantial depletion of the TFIIIB70
polypeptide was detected by Western immunoblot analysis of extracts
derived from cycloheximide growth-arrested cells, indicating that the
inactivation of this TFIIIB component results primarily from its
enhanced destabilization under conditions of protein synthesis
inhibition.
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