Cloning of a cDNA encoding a human DNA-binding protein similar to ribosomal protein S1

Elizabeth A. Eklund, Seung won Lee, David G. Skalnik*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

We report the cloning of a human complementary DNA that encodes a protein which exhibits 36% identity and 62% similarity to Escherichia coli ribosomal protein S1 (rpS1), including conservation of four copies of an RNA-binding domain. This clone was obtained by ligand-screening a λgt11 expression library with a DNA probe derived from the CYBB gene promoter. Electrophoretic mobility shift and Southwestern blot assays confirm DNA binding activity of the protein, which exhibits preferential binding to single-stranded and double-stranded DNA and a low binding affinity for RNA. Hence, the rpS1 protein domain previously identified as an RNA-binding motif can also serve as a DNA-binding domain.

Original languageEnglish (US)
Pages (from-to)231-235
Number of pages5
JournalGene
Volume155
Issue number2
DOIs
StatePublished - Apr 3 1995

Keywords

  • Escherichia coli
  • Glutathione S-transferase fusion protein
  • Southwestern blot
  • ligand screen

ASJC Scopus subject areas

  • Genetics

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