Journal article
A cysteine residue in helixII of the bHLH domain is essential for homodimerization of the yeast transcription factor Pho4p
Nucleic acids research, Vol.26(3), pp.710-714
01 Feb 1998
PMID: 9443961
Abstract
The yeast transcription factor Pho4p is required for expression of the phosphate-repressible acid phosphatase encoded by the PHO5 gene. Functional studies have shown that the molecule is composed of an N-terminal acidic activation domain, a central region which is necessary for interaction with a negative regulatory factor (the cyclin Pho80) and a C-terminal basic helix-loop-helix domain, which mediates DNA binding and homodimerization. In this study the homodimerization domain maps specifically to helixII of this region and a cysteine residue within this region is essential for this function. Experiments support the role of an intermolecular disulfide bond in stabilization of homodimerization, which is critical for DNA binding.
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Details
- Title
- A cysteine residue in helixII of the bHLH domain is essential for homodimerization of the yeast transcription factor Pho4p
- Creators
- D Shao - Department of Microbiology and Immunology, Allegheny University of the Health Sciences, 2900 Queen Lane, Philadelphia, PA 19102, USAC L Creasy - Department of Microbiology and Immunology, Allegheny University of the Health Sciences, 2900 Queen Lane, Philadelphia, PA 19102, USAL W Bergman - Department of Microbiology and Immunology, Allegheny University of the Health Sciences, 2900 Queen Lane, Philadelphia, PA 19102, USA
- Publication Details
- Nucleic acids research, Vol.26(3), pp.710-714
- Publisher
- Oxford University Press
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Identifiers
- 991014878108404721
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- Web of Science research areas
- Biochemistry & Molecular Biology