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  • Molecular Sequence Data  (2)
  • Instrumentation and Photography
  • American Association for the Advancement of Science (AAAS)  (2)
  • 1
    Publikationsdatum: 2002-07-06
    Beschreibung: Blue light regulates many physiological processes in fungi, but their photoreceptors are not known. In Neurospora crassa, all light responses depend on the Per-Arnt-Sim (PAS) domain-containing transcription factor white collar-1 (wc-1). By removing the WC-1 light, oxygen, or voltage domain, a specialized PAS domain that binds flavin mononucleotide in plant phototropins, we show that light responses are abolished, including light entrainment of the circadian clock. However, the WC-1-mediated dark activation of frq remains normal in this mutant, and the circadian clock can be entrained by temperature. Furthermore, we demonstrate that the purified Neurospora WC-1-WC-2 protein complex is associated with stoichiometric amounts of the chromophore flavin-adenine dinucleotide. Together, these observations suggest that WC-1 is the blue-light photoreceptor for the circadian clock and other light responses in Neurospora.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉He, Qiyang -- Cheng, Ping -- Yang, Yuhong -- Wang, Lixing -- Gardner, Kevin H -- Liu, Yi -- New York, N.Y. -- Science. 2002 Aug 2;297(5582):840-3. Epub 2002 Jul 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12098705" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Circadian Rhythm/radiation effects ; Color ; DNA, Fungal/genetics/metabolism ; DNA-Binding Proteins/chemistry/deficiency/genetics/*metabolism ; Darkness ; Dimerization ; Flavin Mononucleotide/metabolism ; Flavin-Adenine Dinucleotide/metabolism ; Fungal Proteins/chemistry/genetics/metabolism ; Gene Deletion ; Gene Expression Regulation, Fungal/radiation effects ; *Light ; Molecular Sequence Data ; Neurospora crassa/genetics/*metabolism/radiation effects ; Oxygen/metabolism ; Photoreceptors, Microbial/chemistry/genetics/*metabolism ; Promoter Regions, Genetic/genetics ; Protein Binding ; Protein Structure, Tertiary ; Response Elements/genetics ; Temperature ; Transcription Factors/chemistry/deficiency/genetics/*metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1996-01-19
    Beschreibung: Small proteins or protein domains generally require disulfide bridges or metal sites for their stabilization. Here it is shown that the beta beta alpha architecture of zinc fingers can be reproduced in a 23-residue polypeptide in the absence of metal ions. The sequence was obtained through an iterative design process. A key feature of the final design is the incorporation of a type II' beta turn to aid in beta-hairpin formation. Nuclear magnetic resonance analysis reveals that the alpha helix and beta hairpin are held together by a defined hydrophobic core. The availability of this structural template has implications for the development of functional polypeptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Struthers, M D -- Cheng, R P -- Imperiali, B -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):342-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553067" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Circular Dichroism ; DNA-Binding Proteins/chemistry ; *Genes, Synthetic ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Peptides/*chemistry ; *Protein Engineering ; Protein Folding ; Protein Structure, Secondary ; *Protein Structure, Tertiary ; Proteins/*chemistry ; Transcription Factors/chemistry ; Zinc Fingers
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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