Temporal patterns in lacustrine stable isotopes as evidence for climate change during the late glacial in the Southern European Alps

We investigated oxygen and carbon isotopes of bulk carbonate and of benthic freshwater ostracods (Candona candida) in a sediment core of Lago Piccolo di Avigliana that was previously analyzed for pollen and loss-on-ignition, in order to reconstruct environmental changes during the late glacial and early Holocene. The depth-age relationship of the sediment core was established using 14 AMS C-14 dates and the Laacher See Tephra. While stable isotopes of bulk carbonates may have been affected by detrital input and, therefore, only indirectly reflect climatic changes, isotopes measured on ostracod shells provide unambiguous evidence for major environmental changes. Oxygen isotope ratios of ostracod shells (delta O-18(C)) increased by similar to 6 parts per thousand at the onset of the Bolling (similar to 14,650 cal BP) and were similar to 2 parts per thousand lower during the Younger Dryas (similar to 12,850 to 11,650 cal BP), indicating a temporal pattern of climate changes similar to the North Atlantic region. However, in contrast to records in that region, delta O-18(C) gradually decreased during the early Holocene, suggesting that compared to the Younger Dryas more humid conditions occurred and that the lake received gradually increasing input of O-18-depleted groundwater or river water.

Isolation and functional characterization of a stable complex between photoactivated rhodopsin and the G protein, transducin

Transitory binding between photoactivated rhodopsin (Rho* or Meta II) and the G protein transducin (Gt-GDP) is the first step in the visual signaling cascade. Light causes photoisomerization of the 11-cis-retinylidene chromophore in rhodopsin (Rho) to all-trans-retinylidene, which induces conformational changes that allow Gt-GDP to dock onto the Rho* surface. GDP then dissociates from Gt, leaving a transient nucleotide-empty Rho*-Gt(e) complex before GTP becomes bound, and Gt-GTP then dissociates from Rho*. Further biochemical advances are required before structural studies of the various Rho*-Gt complexes can be initiated. Here, we describe the isolation of n-dodecyl-beta-maltoside solubilized, stable, functionally active, Rho*-Gt(e), Rho(e)*-Gt(e), and 9-cis-retinal/11-cis-retinal regenerated Rho-Gt(e) complexes by sucrose gradient centrifugation. In these complexes, Rho* spectrally remained in its Meta II state, and Gt(e) retained its ability to interact with GTPgammaS. Removal of all-trans-retinylidene from Rho*-Gt(e) had no effect on the stability of the Rho(e)*-Gt(e) complex. Moreover, opsin in the Rho(e)*-Gt(e) complex with an empty nucleotide-binding pocket in Gt and an empty retinoid-binding pocket in Rho was regenerated up to 75% without complex dissociation. These results indicate that once Rho* couples with Gt, the chromophore plays a minor role in stabilizing this complex. Moreover, in complexes regenerated with 9-cis-retinal/11-cis-retinal, Rho retains a conformation similar to Rho* that is stabilized by Gt(e) apo-protein.