A C-terminal proline is required for bioluminescence of the Ca2+-binding photoprotein, aequorin
نویسندگان
چکیده
منابع مشابه
Bioluminescence of the Ca(2+)-binding photoprotein, aequorin, after histidine modification.
Modification studies of the 5 histidine residues in aequorin employing site-directed mutagenesis and diethyl pyrocarbonate suggested that His169 may be the site of binding of molecular oxygen in aequorin. The modification of this residue led to complete loss of activity, whereas modification of the remaining 4 histidine residues yielded mutant aequorins with varying bioluminescence activities.
متن کاملSite-specific mutagenesis of the calcium-binding photoprotein aequorin.
The luminescent protein aequorin from the jellyfish Aequoria victoria emits light by an intramolecular reaction in the presence of a trace amount of Ca(2+). In order to understand the mechanism of the reaction, a study of structure-function relationships was undertaken with respect to modifying certain of its amino acid residues. This was done by carrying out oligonucleotide-directed site-speci...
متن کاملCrystal structure of a Ca2+-discharged photoprotein: implications for mechanisms of the calcium trigger and bioluminescence.
Ca2+-regulated photoproteins are members of the EF-hand calcium-binding protein family. The addition of Ca2+ produces a blue bioluminescence by triggering a decarboxylation reaction of protein-bound hydroperoxycoelenterazine to form the product, coelenteramide, in an excited state. Based on the spatial structures of aequorin and several obelins, we have postulated mechanisms for the Ca2+ trigge...
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The dopamine transporter mediates reuptake of dopamine from the synaptic cleft. The cellular mechanisms controlling dopamine transporter levels in striatal nerve terminals remain poorly understood. The dopamine transporters contain a C-terminal PDZ (PSD-95/Discs-large/ZO-1) domain-binding sequence believed to bind synaptic scaffolding proteins, but its functional significance is uncertain. Here...
متن کاملPeroxidized coelenterazine, the active group in the photoprotein aequorin.
The photoprotein aequorin emits light by an intramolecular reaction when Ca2+ is added under either aerobic or anaerobic conditions. Previously reported evidence has indicated two possibilities: (i) the functional group of aequorin is coelenterazine itself, a compond that plays key roles in the bioluminescence of various other types of organisms, or (ii) it is the enolized form of this compound...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1991
ISSN: 0014-5793
DOI: 10.1016/0014-5793(91)81385-l