Nucleic Acids Research, Vol 24, Issue 19 3677-3684, Copyright © 1996 by Oxford University Press
EE Sander, SW Mason, C Munz and I Grummt
The transcription termination factor TTF-I binds specifically to an 18 bp
DNA element in the murine ribosomal gene spacer and mediates termination of
RNA polymerase I transcription. In this study, we have compared DNA binding
and termination activity of recombinant full- length TTF-I (TTF-Ip130) with
two deletion mutants lacking 184 and 322 N-terminal amino acids,
respectively. All three proteins exhibit similar termination activity, but
the DNA binding of TTF-Ip130 is at least one order of magnitude lower than
that of the deletion mutants, indicating that the N-terminus represses the
interaction of TTF-I with DNA. The inhibitory effect of the N-terminus can
be transferred to a heterologous DNA binding domain and is separable from
other activities of TTF-I. We show by several methods that TTF-Ip130, the
N-terminal domain alone, and fusions of the N-terminus with the DNA binding
domain of Oct2.2 form stable oligomers in solution. Thus, in contrast to
previous studies suggesting that activation of TTF-I occurs through
proteolysis, we demonstrate that full-length TTF-I mediates termination of
rDNA transcription in vivo and in vitro and that the oligomerization state
of TTF-I may influence its DNA binding activity.
ARTICLES
The amino-terminal domain of the transcription termination factor TTF-I causes protein oligomerization and inhibition of DNA binding
Division of Molecular Biology of the Cell II, German Cancer Research Center, Heidelberg, Germany.
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