Mutants of GAL4 protein altered in an activation function - PubMed (original) (raw)

Mutants of GAL4 protein altered in an activation function

G Gill et al. Cell. 1987.

Abstract

Activating region I of GAL4 has been defined as a region 48 amino acids long which, when attached to GAL4's DNA-binding domain, activates transcription in yeast. Here we describe mutants bearing changes in and around this highly acidic activating region. We find mutations that increase the activation function invariably increase the acidity of the region and some but not all of the mutations that decrease the activation function decrease the acidity of the region.

PubMed Disclaimer

Similar articles

• A new class of yeast transcriptional activators.
  Ma J, Ptashne M. Ma J, et al. Cell. 1987 Oct 9;51(1):113-9. doi: 10.1016/0092-8674(87)90015-8. Cell. 1987. PMID: 3115591
• Separation of DNA binding from the transcription-activating function of a eukaryotic regulatory protein.
  Keegan L, Gill G, Ptashne M. Keegan L, et al. Science. 1986 Feb 14;231(4739):699-704. doi: 10.1126/science.3080805. Science. 1986. PMID: 3080805
• Wild type GAL4 binds cooperatively to the GAL1-10 UASG in vitro.
  Kang T, Martins T, Sadowski I. Kang T, et al. J Biol Chem. 1993 May 5;268(13):9629-35. J Biol Chem. 1993. PMID: 8486650
• Gene identification using the yeast two-hybrid system.
  Bai C, Elledge SJ. Bai C, et al. Methods Enzymol. 1996;273:331-47. doi: 10.1016/s0076-6879(96)73029-x. Methods Enzymol. 1996. PMID: 8791622 Review. No abstract available.
• Nutrients and gene expression.
  De Caterina R, Madonna R, Hassan J, Procopio AD. De Caterina R, et al. World Rev Nutr Diet. 2001;89:23-52. doi: 10.1159/000059790. World Rev Nutr Diet. 2001. PMID: 11530735 Review. No abstract available.

Cited by

• The intrinsically disordered transcriptional activation domain of CIITA is functionally tuneable by single substitutions: An exception or a new paradigm?
  Sreenivasan S, Heffren P, Suh KS, Rodnin MV, Kosa E, Fenton AW, Ladokhin AS, Smith PE, Fontes JD, Swint-Kruse L. Sreenivasan S, et al. Protein Sci. 2024 Feb;33(2):e4863. doi: 10.1002/pro.4863. Protein Sci. 2024. PMID: 38073129 Free PMC article.
• Effects of high mobility group proteins 1 and 2 on initiation and elongation of specific transcription by RNA polymerase II in vitro.
  Tremethick DJ, Molloy PL. Tremethick DJ, et al. Nucleic Acids Res. 1988 Dec 9;16(23):11107-23. doi: 10.1093/nar/16.23.11107. Nucleic Acids Res. 1988. PMID: 2462724 Free PMC article.
• Roles of two activation domains in Zap1 in the response to zinc deficiency in Saccharomyces cerevisiae.
  Frey AG, Eide DJ. Frey AG, et al. J Biol Chem. 2011 Feb 25;286(8):6844-54. doi: 10.1074/jbc.M110.203927. Epub 2010 Dec 22. J Biol Chem. 2011. PMID: 21177862 Free PMC article.
• Yeast nucleotide excision repair proteins Rad2 and Rad4 interact with RNA polymerase II basal transcription factor b (TFIIH).
  Bardwell AJ, Bardwell L, Iyer N, Svejstrup JQ, Feaver WJ, Kornberg RD, Friedberg EC. Bardwell AJ, et al. Mol Cell Biol. 1994 Jun;14(6):3569-76. doi: 10.1128/mcb.14.6.3569-3576.1994. Mol Cell Biol. 1994. PMID: 8196602 Free PMC article.
• Interactions among three proteins that specifically activate translation of the mitochondrial COX3 mRNA in Saccharomyces cerevisiae.
  Brown NG, Costanzo MC, Fox TD. Brown NG, et al. Mol Cell Biol. 1994 Feb;14(2):1045-53. doi: 10.1128/mcb.14.2.1045-1053.1994. Mol Cell Biol. 1994. PMID: 8289785 Free PMC article.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Elsevier Science

• Other Literature Sources

  • The Lens - Patent Citations Database

• Molecular Biology Databases

  • BioCyc
  • Saccharomyces Genome Database