Site-directed mutagenesis of arginine 246, glutamic acid 247, and histidine 248 in the eukaryotic transcription factor S-II

Nobuo Horikoshi, Kazuhisa Sekimizu, Shunji Natori*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

When His248 of the transcription factor S-II was replaced by alanine or tyrosine, the activity of the resulting mutants was less than 30% of that of the wild-type S-II. When Arg246, Glu247, and His248 were all replaced by leucine, the resulting mutant showed complete loss of activity. These results indicate that the amino acid sequence Arg-Glu-His at positions 246-248 of S-II is important for its stimulatory activity. The mutant S-II with no activity could not form a complex with RNA polymerase II, unlike wild-type S-II, but retained ability to interact with DNA.

Original languageEnglish (US)
Pages (from-to)11854-11857
Number of pages4
JournalJournal of Biological Chemistry
Volume265
Issue number20
StatePublished - 1990

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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