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Nucleic Acids Research, 2001, Vol. 29, No. 3 767-773
© 2001 Oxford University Press

Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription

Sheng-Hao Chao1, Arno L. Greenleaf2 and David H. Price1,3,*

1Molecular Biology Program, University of Iowa, Iowa City, IA 52242, USA, 2Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA and 3Department of Biochemistry, University of Iowa, Iowa City, IA 52242, USA

The C-terminal domain (CTD) of the large subunit of RNA polymerase II plays a role in transcription and RNA processing. Yeast ESS1, a peptidyl-prolyl cis/trans isomerase, is involved in RNA processing and can associate with the CTD. Using several types of assays we could not find any evidence of an effect of Pin1, the human homolog of ESS1, on transcription by RNA polymerase II in vitro or on the expression of a reporter gene in vivo. However, an inhibitor of Pin1, 5-hydroxy-1,4-naphthoquinone (juglone), blocked transcription by RNA polymerase II. Unlike N-ethylmaleimide, which inhibited all phases of transcription by RNA polymerase II, juglone disrupted the formation of functional preinitiation complexes by modifying sulfhydryl groups but did not have any significant effect on either initiation or elongation. Both RNA polymerases I and III, but not T7 RNA polymerase, were inhibited by juglone. The primary target of juglone has not been unambiguously identified, although a site on the polymerase itself is suggested by inhibition of RNA polymerase II during factor-independent transcription of single-stranded DNA. Because of its unique inhibitory properties juglone should prove useful in studying transcription in vitro.

* To whom correspondence should be addressed at: Department of Biochemistry, University of Iowa, Iowa City, IA 52242, USA. Tel: +1 319 335 7910; Fax: +1 319 335 9570; Email: david-price{at}uiowa.edu


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