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Crystallization and X-ray diffraction data of a tRNASec acceptor-stem helix (1999)

Förster, Charlotte ; Eickmann, Andrea ; Schubert, Uwe ; [et al.]

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 55 (1999), S. 664-666

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ISSN: 1399-0047

Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Topics: Chemistry and Pharmacology , Geosciences , Physics

Notes: tRNASec is a UGA suppressor tRNA which co-translationally inserts selenocysteine into proteins. Its eight-base-pair tRNASec acceptor stem, which contains key recognition elements, was synthesized using solid-phase phosphoramidite RNA chemistry. High-resolution X-ray diffraction data were collected using synchrotron radiation under cryogenic cooling conditions. The crystals diffract to a maximal resolution of 1.8 Å. X-ray diffraction data were processed to 2.4 Å. tRNASec microhelix crystallizes in space group R32, with cell constants a = 47.02, b = 47.02, c = 373.03 Å, α = β = 90, γ = 120°. The crystals contain three RNA molecules per asymmetric unit.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1107/S0907444998007094

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The synaptophysin/synaptobrevin interaction critically depends on the cholesterol content (2003)

Mitter, Diana ; Reisinger, Clemens ; Hinz, Britta ; [et al.]

Oxford, UK : Blackwell Science Ltd

Journal of neurochemistry 84 (2003), S. 0

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ISSN: 1471-4159

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: Synaptophysin interacts with synaptobrevin in membranes of adult small synaptic vesicles. The synaptophysin/synaptobrevin complex promotes synaptobrevin to built up functional SNARE complexes thereby modulating synaptic efficiency. Synaptophysin in addition is a cholesterol-binding protein. Depleting the membranous cholesterol content by filipin or β-methylcyclodextrin (β-MCD) decreased the solubility of synaptophysin in Triton X-100 with less effects on synaptobrevin. In small synaptic vesicles from rat brain the synaptophysin/synaptobrevin complex was diminished upon β-MCD treatment as revealed by chemical cross-linking. Mice with a genetic mutation in the Niemann–Pick C1 gene developing a defect in cholesterol sorting showed significantly reduced amounts of the synaptophysin/synaptobrevin complex compared to their homo- or heterozygous littermates. Finally when using primary cultures of mouse hippocampus the synaptophysin/synaptobrevin complex was down-regulated after depleting the endogenous cholesterol content by the HMG-CoA-reductase inhibitor lovastatin. Alternatively, treatment with cholesterol up-regulated the synaptophysin/synaptobrevin interaction in these cultures. These data indicate that the synaptophysin/synaptobrevin interaction critically depends on a high cholesterol content in the membrane of synaptic vesicles. Variations in the availability of cholesterol may promote or impair synaptic efficiency by interfering with this complex.