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Cryptic DNA-binding domain in the C terminus of RNA polymerase II general transcription factor RAP30.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 1994 Oct 11; Vol. 91 (21), pp. 9808-12. - Publication Year :
- 1994
-
Abstract
- The C terminus of mammalian transcription factor RAP30 has been found to be a cryptic DNA-binding domain strikingly similar to the C-terminal DNA-binding domain present in conserved region 4 of members of the sigma 70 family of bacterial sigma factors. This RAP30 domain shares strongest sequence similarity with the DNA-binding domain present in region 4 of Bacillus subtilis sporulation-specific sigma K. Like the region 4 DNA-binding activity of Escherichia coli sigma 70, the RAP30 C-terminal DNA binding activity is masked in intact RAP30 but is readily detectable when the RAP30 C terminus is expressed as a fusion protein. Consistent with a role for RAP30 DNA-binding activity in transcription, mutations that abolish DNA binding also abolish transcription. Therefore, RAP30 may function at least in part through the action of an evolutionarily ancient DNA-binding domain that first appeared prior to the divergence of bacteria and eukaryotes.
- Subjects :
- Amino Acid Sequence
Animals
Bacillus subtilis metabolism
Base Sequence
Binding Sites
Carrier Proteins biosynthesis
Carrier Proteins metabolism
Cloning, Molecular
DNA-Binding Proteins isolation & purification
Escherichia coli metabolism
Maltose-Binding Proteins
Mammals
Molecular Sequence Data
Recombinant Fusion Proteins isolation & purification
Recombinant Fusion Proteins metabolism
Sigma Factor metabolism
Transcription Factors biosynthesis
Transcription Factors isolation & purification
Transcription, Genetic
ATP-Binding Cassette Transporters
DNA metabolism
DNA-Binding Proteins metabolism
Escherichia coli Proteins
Monosaccharide Transport Proteins
Oligodeoxyribonucleotides metabolism
RNA Polymerase II metabolism
Transcription Factors metabolism
Transcription Factors, TFII
Subjects
Details
- Language :
- English
- ISSN :
- 0027-8424
- Volume :
- 91
- Issue :
- 21
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 7937895
- Full Text :
- https://doi.org/10.1073/pnas.91.21.9808