Nucleic Acids Research, Vol 25, Issue 6 1142-1147, Copyright © 1997 by Oxford University Press
EE Sander and I Grummt
Mammalian ribosomal genes are flanked at their 5'and 3'ends by terminator
sequences which are recognized by the transcription termination factor
TTF-I. The occurrence of the same binding site upstream and downstream of
the gene raises the possibility that TTF-I can interact with both sequences
simultaneously and thus brings the terminator in the vicinity of the gene
promoter by looping out the pre- rRNA coding sequence. To test this model,
we have examined the ability of TTF-I to oligomerize and found that both
full-length and N- terminally truncated versions of TTF-I form stable
oligomeric structures. At least two domains of TTF-I located within the 184
N- terminal and 445 C-terminal amino acids, respectively, mediate the self-
association of several TTF-I molecules. In support of the looping model,
TTF-I is capable of linking two separate DNA fragments via binding to the
target sites. This result indicates that in addition to its function in
transcription termination, TTF-I may serve a role in the structural
organization of the ribosomal genes which may be important for maintaining
the high loading density of RNA polymerase I on active rRNA genes.
ARTICLES
Oligomerization of the transcription termination factor TTF-I: implications for the structural organization of ribosomal transcription units
Division of Molecular Biology of the Cell II, German Cancer Research Center, D-69120 Heidelberg, Germany.
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