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Nucleic Acids Research, 1992, Vol. 20, No. 12 3121-3125
© 1992

MOLECULAR BIOLOGY

Joints formed by RecA protein from oligonucleotides and duplex DNA block initiation and elongation of transcription

Efim l. Golub, David C. Ward and Charles M. Radding

The Departments of Genetics and Molecular Biophysics & Biochemistry, Yale Universfty School of Medicine New Haven, CT 06510, USA

Received February 27, 1992. Accepted May 20, 1992.

In the presence of the non-hydrolyzable analog of ATP, ATP{gamma}S, RecA protein can polymerize on an oligodeoxyribonucleotide to form a stable oligonucleoprotein filament that can find its homologous sequence in double-stranded DNA. The homologous joint formed by the oligonucleotide and duplex DNA is stable only if RecA protein is not removed. Such a nucleoprotein joint, covering a part or all of the promoter region of T3 or T7 phage RNA polymerase, blocked transcription directed by those polymerases. The same kind of joint, located downstream of the RNA polymerase promoter, also inhibited elongation of transcription and caused accumulation of truncated transcripts. These observations suggest that RecA protein can be used to shut off transcription from any promoter of known sequence.


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