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. 1989 Oct 5;341(6241):410-4.
doi: 10.1038/341410a0.

Structure and associated DNA-helicase activity of a general transcription initiation factor that binds to RNA polymerase II

M Sopta  1 , Z F Burton, J Greenblatt
Affiliations

Structure and associated DNA-helicase activity of a general transcription initiation factor that binds to RNA polymerase II

M Sopta et al. Nature. .

Abstract

RAP30/74 is a heteromeric general transcription initiation factor which binds to RNA polymerase II. Here we report that preparations of RAP30/74 contain an ATP-dependent DNA helicase whose probable function is to melt the DNA at transcriptional start sites. The sequence of the RAP30 subunit of RAP30/74 indicates that RAP30 may be distantly related to bacterial sigma factors.

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