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 language | English (US) |
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Pages (from-to) | 231-235 |
Number of pages | 5 |
Journal | Gene |
Volume | 155 |
Issue number | 2 |
DOIs | |
State | Published - Apr 3 1995 |
Funding
We thank Mark Kelley and Ira Wool for helpful discussions regarding multifunctional ribosomal proteins, Yi Xu for providing RNA probes, and Riley Children's Cancer Research for supporting oligonucleotide synthesis. This work was supported by the Riley Memorial Association, and by the following grants awarded to D.G.S.: NIH No. 1 R29 CA58947, American Cancer Society No. JFRA 421, a National Leukemia Association Grant and a grant by the Project Development Program, Research and Sponsored Programs, Indiana University at Indianapolis. E.A.E. and S.-w.L. were supported by the Walther Oncology Center.
Keywords
- Escherichia coli
- Glutathione S-transferase fusion protein
- Southwestern blot
- ligand screen
ASJC Scopus subject areas
- Genetics