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EMBO Rep. 2002 Feb;3(2):147-52. Epub 2002 Jan 29.

Transcription termination factor TTF-I exhibits contrahelicase activity during DNA replication.

Author information

1
Institute of Biochemistry, University of Würzburg, D-97074 Würzburg, Germany.

Abstract

In mammals, sequence-specific termination of DNA replication within the ribosomal RNA genes is catalyzed by a defined DNA-protein complex that includes transcription termination factor I (TTF-I). Here we show that TTF-I acts as a polar contrahelicase contrary to the intrinsic 3' -->5' helicase activity of SV40 large T antigen. The contrahelicase activity requires binding of TTF-I to its cognate recognition site and the presence of an auxiliary GC-rich sequence, which is able to form a specific secondary structure. Mutations in the GC-rich sequence lead to a loss of folding into correct secondary structure and abrogate contrahelicase activity. The finding suggests that a specific interaction between the Sal box-bound TTF-I and the GC-rich sequence is essential for the inhibition of T antigen helicase. Analyses of N-terminally truncated mutants of TTF-I showed inhibition of helicase by the same domain of TTF-I, which is also responsible for replication fork arrest.

PMID:
11818337
PMCID:
PMC1083968
DOI:
10.1093/embo-reports/kvf027
[Indexed for MEDLINE]
Free PMC Article

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