Home LiteratureArticle Details
PMID: 1498607 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Homodimeric and heterodimeric leucine zipper proteins and nuclear factors from parsley recognize diverse promoter elements with ACGT cores.

The Plant cell ·Vol. 4 ·No. 5 ·1992-05-00 ·Pages 525-37

Armstrong GA, Weisshaar B, Hahlbrock K

Abstract

Four short nucleotide sequences (boxes I to IV) contribute to the light responsiveness of the parsley chalcone synthase promoter. The sequence-related boxes II and III resemble several plant, viral, and bacterial promoter elements that share ACGT core sequences and are associated with diversely regulated genes. We have analyzed the binding characteristics and protein-protein interactions of factors from nuclear extracts and of three putative leucine zipper (bZIP) transcription factors potentially involved in the regulation of this promoter. These common plant regulatory factors (CPRFs) bind specifically to boxes II and III as well as other ACGT-containing promoter elements (hex1, Em1a, and as-1), though with markedly different affinities. Intact bZIP domains are crucial for CPRF binding to DNA. Distinct ensembles of nuclear factors bind to boxes II and III, despite their sequence similarity. The parsley CPRFs bind to DNA as dimers, selectively form heterodimeric DNA binding complexes, and interact with nuclear proteins.

MeSH Terms
Acyltransferases/genetics Amino Acid Sequence Base Sequence DNA DNA-Binding Proteins/metabolism Gene Expression Regulation, Enzymologic/radiation effects Leucine Zippers Light Molecular Sequence Data Nuclear Proteins/metabolism Plant Proteins/metabolism Plants/genetics Promoter Regions, Genetic
Chemicals
CPRF protein, Petroselinum crispum DNA-Binding Proteins Nuclear Proteins Plant Proteins DNA Acyltransferases flavanone synthetase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Armstrong G A
Max-Planck-Institut für Züchtungsforschung, Abteilung Biochemie, Köln, Germany.
Weisshaar B
Hahlbrock K
References (35)
35 references, click to expand
  1. Purification of tobacco nuclear proteins binding to a CACGTG motif of the chalcone synthase promoter by DNA affinity chromatography.
    Eur J Biochem. 1991 Aug 1;199(3):519-27 PMID: 1714388
  2. Parsley protoplasts retain differential responsiveness to u.v. light and fungal elicitor.
    EMBO J. 1987 Sep;6(9):2551-6 PMID: 16453792
  3. Toward an understanding of plant gene regulation: the action of nuclear factors.
    Z Naturforsch C. 1991 Jan-Feb;46(1-2):1-11 PMID: 2039578
  4. A tobacco bZip transcription activator (TAF-1) binds to a G-box-like motif conserved in plant genes.
    EMBO J. 1991 Jul;10(7):1793-802 PMID: 2050116
  5. A plant leucine zipper protein that recognizes an abscisic acid response element.
    Science. 1990 Oct 12;250(4978):267-71 PMID: 2145628
  6. Molecular light switches for plant genes.
    Plant Cell. 1990 May;2(5):369-78 PMID: 2152164
  7. The plant G box promoter sequence activates transcription in Saccharomyces cerevisiae and is bound in vitro by a yeast activity similar to GBF, the plant G box binding factor.
    EMBO J. 1990 Jun;9(6):1727-35 PMID: 2161333
  8. Functional borders, genetic fine structure, and distance requirements of cis elements mediating light responsiveness of the parsley chalcone synthase promoter.
    Proc Natl Acad Sci U S A. 1990 Jul;87(14):5387-91 PMID: 2371277
  9. Regulation of eukaryotic transcription factors by post-translational modification.
    Biochim Biophys Acta. 1989 Nov 2;1009(2):103-9 PMID: 2529903
  10. Inducible in vivo DNA footprints define sequences necessary for UV light activation of the parsley chalcone synthase gene.
    EMBO J. 1989 Mar;8(3):651-6 PMID: 2566481
  11. Scissors-grip model for DNA recognition by a family of leucine zipper proteins.
    Science. 1989 Nov 17;246(4932):911-6 PMID: 2683088
  12. A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein.
    Proc Natl Acad Sci U S A. 1989 Sep;86(18):6930-4 PMID: 2780550
  13. An evolutionarily conserved protein binding sequence upstream of a plant light-regulated gene.
    Proc Natl Acad Sci U S A. 1988 Oct;85(19):7089-93 PMID: 2902624
  14. The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins.
    Science. 1988 Jun 24;240(4860):1759-64 PMID: 3289117
  15. In situ localization of light-induced chalcone synthase mRNA, chalcone synthase, and flavonoid end products in epidermal cells of parsley leaves.
    Proc Natl Acad Sci U S A. 1988 May;85(9):2989-93 PMID: 16578833
  16. Diversity and specificity in transcriptional regulation: the benefits of heterotypic dimerization.
    Trends Biochem Sci. 1991 Nov;16(11):417-22 PMID: 1776171
  17. Regulatory elements required for light-mediated expression of the Petroselinum crispum chalcone synthase gene.
    Symp Soc Exp Biol. 1991;45:191-210 PMID: 1843408
  18. The maize regulatory locus Opaque-2 encodes a DNA-binding protein which activates the transcription of the b-32 gene.
    EMBO J. 1991 Mar;10(3):617-24 PMID: 2001677
  19. HBP-1a and HBP-1b: leucine zipper-type transcription factors of wheat.
    EMBO J. 1991 Jun;10(6):1459-67 PMID: 2026143
  20. Light-inducible and constitutively expressed DNA-binding proteins recognizing a plant promoter element with functional relevance in light responsiveness.
    EMBO J. 1991 Jul;10(7):1777-86 PMID: 2050115
  21. Integrity of FOS B leucine zipper is essential for its interaction with JUN proteins.
    Oncogene. 1990 Jul;5(7):1091-3 PMID: 2115643
  22. In vivo and in vitro characterization of protein interactions with the dyad G-box of the Arabidopsis Adh gene.
    Plant Cell. 1990 Mar;2(3):207-14 PMID: 2152112
  23. OCSBF-1, a maize ocs enhancer binding factor: isolation and expression during development.
    Plant Cell. 1990 Sep;2(9):891-903 PMID: 2152133
  24. Characterization of the Arabidopsis Adh G-box binding factor.
    Plant Cell. 1990 Jun;2(6):547-57 PMID: 2152176
  25. Dimers, leucine zippers and DNA-binding domains.
    Trends Genet. 1990 Feb;6(2):36-40 PMID: 2186528
  26. Mutation of either G box or I box sequences profoundly affects expression from the Arabidopsis rbcS-1A promoter.
    EMBO J. 1990 Jun;9(6):1717-26 PMID: 2347304
  27. Sequence-specific DNA binding by a short peptide dimer.
    Science. 1990 Aug 17;249(4970):769-71 PMID: 2389142
  28. Abscisic acid-responsive sequences from the em gene of wheat.
    Plant Cell. 1989 Oct;1(10):969-76 PMID: 2562556
  29. The ocs-element is a component of the promoters of several T-DNA and plant viral genes.
    EMBO J. 1989 Dec 20;8(13):4197-204 PMID: 2591372
  30. Eukaryotic transcriptional regulatory proteins.
    Annu Rev Biochem. 1989;58:799-839 PMID: 2673023
  31. A protein that binds to a cis-acting element of wheat histone genes has a leucine zipper motif.
    Science. 1989 Sep 1;245(4921):965-7 PMID: 2772648
  32. Site-specific mutations alter in vitro factor binding and change promoter expression pattern in transgenic plants.
    Proc Natl Acad Sci U S A. 1989 Oct;86(20):7890-4 PMID: 2813365
  33. Two alleles of the single-copy chalcone synthase gene in parsley differ by a transposon-like element.
    Mol Gen Genet. 1988 Apr;212(1):93-8 PMID: 2836708
  34. Evidence that the leucine zipper is a coiled coil.
    Science. 1989 Jan 27;243(4890):538-42 PMID: 2911757
  35. Non-leucine residues in the leucine repeats of Fos and Jun contribute to the stability and determine the specificity of dimerization.
    Nucleic Acids Res. 1991 Feb 25;19(4):739-46 PMID: 1901988
Article Info
Journal
The Plant cell
Abbr.
Plant Cell
ISSN
1040-4651
Published
1992-05-00
Pages
525-37
Language
English
Region
England
NLM ID
9208688
PMCID
PMC160150
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]