Similarity of DNA-recognizing structures of the coordinated transcription activator of yeast amino acid biosynthesis enzymes genes, yeast cells differentiation regulators, development and morphogenesis regulators

Shestopalov, B. V.

doi:10.7124/bc.000238

Biopolym. Cell. 1988; 4(5):272-274.

http://dx.doi.org/10.7124/bc.000238

Short Communications

Similarity of DNA-recognizing structures of the coordinated transcription activator of yeast amino acid biosynthesis enzymes genes, yeast cells differentiation regulators, development and morphogenesis regulators

1Shestopalov B. V.

Institute of Cytology, Academy of Sciences of the USSR
Leningrad, USSR

Abstract

Basing on the data obtained by the method of necessary stereochemical requirements of the DNA-recognizing structure helix-turn-helix existence and the available data from literature a conclusion is made that 1) GCN4 protein, probably, recognizes DNA using DNA-recognizing structure helix-turn-helix, localized in the amino acid sequence segment 256–278 and 2) DNA-recognizing structure of GCN4 protein is similar to those of MATα1 and MATα2 proteins, and homoeodomain-containing proteins.

Full text: (PDF, in Russian)

References

[1] Hinnebusch AG. Multiple levels of gene regulation in the control of amino acid biosynthesis in Saccharomyces cerevisiae. Bioessays. 1986;5(2):57-62.

[2] Hope IA, Struhl K. GCN4 protein, synthesized in vitro, binds HIS3 regulatory sequences: implications for general control of amino acid biosynthetic genes in yeast. Cell. 1985;43(1):177-88.

[3] Hill DE, Hope IA, Macke JP, Struhl K. Saturation mutagenesis of the yeast his3 regulatory site: requirements for transcriptional induction and for binding by GCN4 activator protein. Science. 1986;234(4775):451-7.

[4] Hope IA, Struhl K. Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of yeast. Cell. 1986;46(6):885-94.

[5] Shestopalov BV. Prediction of the DNA-recognizing supersecondary protein structure, alpha helix-turn-alpha helix, using the modified Ohlendorf-Anderson-Matthews method of necessary stereochemical requirements. Mol Biol (Mosk). 1988;22(2):323-30.

[6] Laughon A, Scott MP. Sequence of a Drosophila segmentation gene: protein structure homology with DNA-binding proteins. Nature. 1984 Jul 5-11;310(5972):25-31.

[7] Shepherd JC, McGinnis W, Carrasco AE, De Robertis EM, Gehring WJ. Fly and frog homoeo domains show homologies with yeast mating type regulatory proteins. Nature. 1984 Jul 5-11;310(5972):70-1.

[8] Porter SD, Smith M. Homoeo-domain homology in yeast MAT alpha 2 is essential for repressor activity. Nature. 1986 Apr 24-30;320(6064):766-8.

[9] Ohlendorf DH, Anderson WF, Matthews BW. Many gene-regulatory proteins appear to have a similar alpha-helical fold that binds DNA and evolved from a common precursor. J Mol Evol. 1983;19(2):109-14.

[10] Poole SJ, Kauvar LM, Drees B, Kornberg T. The engrailed locus of Drosophila: structural analysis of an embryonic transcript. Cell. 1985;40(1):37-43.

[11] Desplan C, Theis J, O'Farrell PH. The Drosophila developmental gene, engrailed, encodes a sequence-specific DNA binding activity. Nature. 1985 Dec 19-1986;318(6047):630-5.

[12] Johnson AD, Herskowitz I. A repressor (MAT alpha 2 Product) and its operator control expression of a set of cell type specific genes in yeast. Cell. 1985;42(1):237-47.

[13] Miller AM, MacKay VL, Nasmyth KA. Identification and comparison of two sequence elements that confer cell-type specific transcription in yeast. Nature. 1985 Apr 18-24;314(6012):598-603.

[14] Fainsod A, Bogarad LD, Ruusala T, Lubin M, Crothers DM, Ruddle FH. The homeo domain of a murine protein binds 5' to its own homeo box. Proc Natl Acad Sci U S A. 1986;83(24):9532-6.