PMID: 9443961Mar 14, 1998Paper

A cysteine residue in helixII of the bHLH domain is essential for homodimerization of the yeast transcription factor Pho4p

Nucleic Acids Research
D ShaoL W Bergman

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.

References

Oct 5, 1989·Journal of Molecular Biology·M CareyM Ptashne
Feb 11, 1994·Nucleic Acids Research·D BarettinoH G Stunnenberg
Jan 20, 1993·Journal of Molecular Biology·T HakoshimaY Oshima

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Citations

Jun 22, 2005·Biochimica Et Biophysica Acta·Mary E GardockiJohn M Lopes
Sep 16, 2006·Nucleic Acids Research·Robert J McDonaldL James Maher
Mar 10, 2005·Eukaryotic Cell·Mary E GardockiJohn M Lopes
May 23, 2014·Journal of Biosciences·Parul Tomar, Himanshu Sinha
Jan 9, 2016·Applied Microbiology and Biotechnology·Anna Judith SchifferdeckerOlena P Ishchuk
Mar 14, 2020·International Journal of Molecular Sciences·Jennifer E G GallagherAmaury Pupo
Nov 5, 1999·Biochimica Et Biophysica Acta·B L PerssonJ Pattison

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