Inhibition of a DNA-helicase by peptide nucleic acids

Lionel Bastide, Paul E Boehmer, Giuseppe Villani, Bernard Lebleu

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Bis-peptide nucleic acid (bis-PNA) binding results in D-loop formation by strand displacement at complementary homopurine stretches in DNA duplexes. Transcription and replication in intact cells is mediated by multienzymatic complexes involving several proteins other than polymerases. The behaviour of the highly stable clamp structure formed by bis-PNAs has thus far been studied with respect to their capacity to arrest RNA polymerases. Little attention has been given to their recognition and processing by DNA helicases. In this report we have investigated the inhibitory effect of a bis-PNA on the DNA-helicase activity of the well characterized herpes simplex type I UL9 protein. Unwinding by UL9 of a synthetic substrate is significantly inhibited by a bis-PNA and the addition of the ICP8 protein, which increases UL9 processivity, does not relieve this inhibition.

Original languageEnglish (US)
Pages (from-to)551-554
Number of pages4
JournalNucleic Acids Research
Volume27
Issue number2
DOIs
StatePublished - Jan 15 1999
Externally publishedYes

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Peptide Nucleic Acids
DNA Helicases
Herpes Simplex
Proteins
DNA-Directed RNA Polymerases
DNA

ASJC Scopus subject areas

  • Genetics

Cite this

Inhibition of a DNA-helicase by peptide nucleic acids. / Bastide, Lionel; Boehmer, Paul E; Villani, Giuseppe; Lebleu, Bernard.

In: Nucleic Acids Research, Vol. 27, No. 2, 15.01.1999, p. 551-554.

Research output: Contribution to journalArticle

Bastide, Lionel ; Boehmer, Paul E ; Villani, Giuseppe ; Lebleu, Bernard. / Inhibition of a DNA-helicase by peptide nucleic acids. In: Nucleic Acids Research. 1999 ; Vol. 27, No. 2. pp. 551-554.
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