Journal article
Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription
Nucleic acids research, Vol.29(3), pp.767-773
02/01/2001
DOI: 10.1093/nar/29.3.767
PMCID: PMC30403
PMID: 11160900
Abstract
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
.
Details
- Title: Subtitle
- Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription
- Creators
- Sheng-Hao Chao - Molecular Biology Program, University of Iowa, Iowa City, IA 52242, USAArno L Greenleaf - Molecular Biology Program, University of Iowa, Iowa City, IA 52242, USADavid H Price - Molecular Biology Program, University of Iowa, Iowa City, IA 52242, USA
- Resource Type
- Journal article
- Publication Details
- Nucleic acids research, Vol.29(3), pp.767-773
- Publisher
- Oxford University Press; Oxford, UK
- DOI
- 10.1093/nar/29.3.767
- PMID
- 11160900
- PMCID
- PMC30403
- ISSN
- 0305-1048
- eISSN
- 1362-4962
- Language
- English
- Date published
- 02/01/2001
- Academic Unit
- Biochemistry and Molecular Biology
- Record Identifier
- 9984025247902771
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