Dramatic loss of microbial viability in bentonite exposed to heat and gamma radiation: implications for deep geological repository.

Bentonite is an integral part of the engineered barrier system (EBS) in deep geological repositories (DGR) for nuclear waste, but its indigenous microorganisms may jeopardize long-term EBS integrity. To predict microbial activity in DGRs, it is essential to understand microbial reactions to the early hot phase of DGR evolution. Two bentonites (BCV and MX-80) with varied bentonite/water ratios and saturation levels (compacted to 1600 kg.

Survivability and proliferation of microorganisms in bentonite with implication to radioactive waste geological disposal: strong effect of temperature and negligible effect of pressure.

As bentonite hosts a diverse spectrum of indigenous microorganisms with the potential to influence the long-term stability of deep geological repositories, it is essential to understand the factors influencing microbial activity under repository conditions. Here, we focus on two factors, i.e.

Sequential inter- and intrasubunit rearrangements during activation of dimeric metabotropic glutamate receptor 1.

The metabotropic glutamate receptor 1 (mGluR1), a class C member of the heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor family, is a constitutive dimer that regulates excitatory neurotransmission. We investigated the role of homodimer formation in mGluR1 activation by examining activation-dependent inter- and intrasubunit conformational changes by fluorescence resonance energy transfer (FRET). We inserted yellow and cyan fluorescent proteins in the second intracellular loop and at the carboxyl terminus of mGluR1 to act as FRET sensors and expressed these proteins in human embryonic kidney 293 cells.

Surface expression of metabotropic glutamate receptor variants mGluR1a and mGluR1b in transfected HEK293 cells.

Class C G-protein coupled receptors form obligatory dimers. Metabotropic glutamate receptors (mGluRs) are found commonly as homodimers. Alternative splicing of mGluR1 gene results in vivo in the expression of a long variant mGluR1a and at least two short variants mGluR1b and d.

Asymmetric functioning of dimeric metabotropic glutamate receptors disclosed by positive allosteric modulators.

The recent discovery of positive allosteric modulators (PAMs) for G-protein-coupled receptors open new possibilities to control a number of physiological and pathological processes. Understanding the mechanism of action of such compounds will provide new information on the activation process of these important receptors. Within the last 10 years, a number of studies indicate that G-protein-coupled receptors can form dimers, but the functional significance of this phenomenon remains elusive.

Evidence for a single heptahelical domain being turned on upon activation of a dimeric GPCR.

G-protein-coupled receptors (GPCRs) have been shown to form dimers, but the relevance of this phenomenon in G-protein activation is not known. Among the large GPCR family, metabotropic glutamate (mGlu) receptors are constitutive dimers. Here we examined whether both heptahelical domains (HDs) are turned on upon full receptor activation.