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  • Base Sequence  (2)
  • American Association for the Advancement of Science (AAAS)  (2)
  • 1
    Publication Date: 2001-01-06
    Description: Plant disease resistance (R) genes control the recognition of specific pathogens and activate subsequent defense responses. We show that the Arabidopsis thaliana locus RESISTANCE TO POWDERY MILDEW8 (RPW8) contains two naturally polymorphic, dominant R genes, RPW8.1 and RPW8.2, which individually control resistance to a broad range of powdery mildew pathogens. Although the predicted RPW8.1 and RPW8.2 proteins are different from the previously characterized R proteins, they induce localized, salicylic acid-dependent defenses similar to those induced by R genes that control specific resistance. Apparently, broad-spectrum resistance mediated by RPW8 uses the same mechanisms as specific resistance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xiao, S -- Ellwood, S -- Calis, O -- Patrick, E -- Li, T -- Coleman, M -- Turner, J G -- New York, N.Y. -- Science. 2001 Jan 5;291(5501):118-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11141561" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Arabidopsis/*genetics/*microbiology/physiology ; *Arabidopsis Proteins ; Ascomycota/growth & development/*pathogenicity ; Base Sequence ; Cosmids ; Genes, Dominant ; *Genes, Plant ; Hydrogen Peroxide/metabolism ; Molecular Sequence Data ; Open Reading Frames ; *Plant Diseases ; Plant Proteins/chemistry/*genetics/physiology ; Plants, Genetically Modified ; Polymorphism, Genetic ; Salicylic Acid/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1995-10-13
    Description: The yeast MAT alpha 2 and MATa1 homeodomain proteins bind cooperatively as a heterodimer to sites upstream of haploid-specific genes, repressing their transcription. In the crystal structure of alpha 2 and a1 bound to DNA, each homeodomain makes independent base-specific contacts with the DNA and the two proteins contact each other through an extended tail region of alpha 2 that tethers the two homeodomains to one another. Because this extended region may be flexible, the ability of the heterodimer to discriminate among DNA sites with altered spacing between alpha 2 and a1 binding sites was examined. Spacing between the half sites was critical for specific DNA binding and transcriptional repression by the complex. However, amino acid insertions in the tail region of alpha 2 suppressed the effect of altering an a1/alpha 2 site by increasing the spacing between the half sites. Insertions in the tail also decreased DNA bending by a1/alpha 2. Thus tethering the two homeodomains contributes to DNA bending by a1/alpha 2, but the precise nature of the resulting bend is not essential for repression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jin, Y -- Mead, J -- Li, T -- Wolberger, C -- Vershon, A K -- GM49265/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 13;270(5234):290-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08855-0759, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569977" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Cloning, Molecular ; DNA, Fungal/chemistry/genetics/*metabolism ; Fungal Proteins/chemistry/*metabolism ; Genes, Fungal ; Homeodomain Proteins/chemistry/*metabolism ; Macromolecular Substances ; Molecular Sequence Data ; Mutagenesis, Insertional ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Repressor Proteins/chemistry/*metabolism ; Saccharomyces cerevisiae/chemistry ; *Saccharomyces cerevisiae Proteins ; Sequence Deletion ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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