Magnetic and gravity measurements on North-South profiles across the Grosse Meteor Bank, North Atlantic

During the first section of the "Meteor" cruise No. 2 a profile was run from the Azores to the south across the flanks of the Mid-Atlantic Ridge with a chain of seamounts. The profile extended between the Cruiser (living) and the Hyeres seamounts, which, according to our soundings, form a connected massif, and across the centre of the Grosse Meteor Bank (30°N, 28.5 °W). These seamounts rise from a depth of more than 4000 m up till close to the surface of the sea forming there a large almost flat plateau. In the case of the Grosse Meteor Bank, this plateau has a N-S extension of approx. 30 nautical miles and an E-W extension of approx. 20 nautical miles and reaches a height of 275 m in water depth. The gravity measurements yielded a density of the topographic masses of 2.6 g/cm**3 for the Grosse Meteor Bank. Magnitude and shape of the measured free-air anomaly are very well shown in a model computation with this density. The theoretical gravity effects of the seismically detected swell of cristalline rock and of the Moho depression (mountain root) are not indicated by the observational data. It can, therefore, be assumed that the latter two neutralize each other. It seems, accordingly, that there is no local isostatic compensation of the topographic masses. Hence, the density of 2.6 g/cm**3 obtained would be about the true density of rock. In connection with the mean velocity of P waves (Aric et al., 1968) obtained by seismic refraction methods it must be concluded that the material of the 1200-4000 m thick surface layer of the Grosse Meteor Bank consists of consolidated sediments. This finding is supported by the total intensity of the Earth's magnetic field over the Grosse Meteor Bank. On the assumption of a homogeneous magnetization in the direction of the present Earth's field, the computed anomaly of the massif deviates considerably from the measured anomaly while the magnetic field of the seismically detected crystalline body is capable of interpreting the observed data. Deviating from the prevailing interpretation of the seamounts' plateau as a volcanic cone with submarine abrasion, the Grosse Meteor Bank and the seamounts in the vicinity are assumed to be of continental origin. The questions whether these seamounts submerged later on or whether the sealevel has risen subsequently are, therefore, largely nonexistent.

Verrucomicrobia in situ abundance and water chemistry in a humic lake during the year 2000

Members of the highly diverse bacterial phylum Verrucomicrobia are globally distributed in various terrestrial and aquatic habitats. They are key players in soils, but little is known about their role in aquatic systems. Thus, we applied newly designed 16S rRNA-targeted probe set for the identification of Verrucomicrobia and of clades within this phylum to a study concerning the seasonal abundance of Verrucomicrobia in waters of the humic lake Große Fuchskuhle (Germany) by catalyzed reporter deposition fluorescence in situ hybridization. The Lake Große Fuchskuhle is located in the large Mecklenburg-Brandenburg lake district near Berlin (53°10'N, 13°02'E). The lake was artificially divided into four basins (northwest, northeast, southwest, and southeast). We chose the two most contrasting basins, the acidotrophic humic southwestern (SW) basin with a high influx of allochthonous dissolved organic carbon (DOC) and the more mesotrophic northeastern (NE) basin, to study abundance and seasonality of Verrucomicrobia. Lake water was collected from depths of 0.5 m (oxic) and 4.5 m (seasonally anoxic) approximately trimonthly in 2000 (March, June, September and December). The lake hosted diverse Verrucomicrobia clades in all seasons. Either Spartobacteria (up to 19%) or Opitutus spp. (up to 7%) dominated the communities, whereas Prosthecobacter spp. were omnipresent in low numbers (<1%). Verrucomicrobial abundance and community composition varied between the seasons, and between more and less humic basins, but were rather stable in oxic and seasonally anoxic waters.

GroEL-GroES-mediated protein folding requires an intact central cavity

The chaperonin GroEL is an oligomeric double ring structure that, together with the cochaperonin GroES, assists protein folding. Biochemical analyses indicate that folding occurs in a cis ternary complex in which substrate is sequestered within the GroEL central cavity underneath GroES. Recently, however, studies of GroEL “minichaperones” containing only the apical substrate binding subdomain have questioned the functional importance of substrate encapsulation within GroEL-GroES complexes. Minichaperones were reported to assist folding despite the fact that they are monomeric and therefore cannot form a central cavity. Here we compare directly the folding activity of minichaperones with that of the full GroEL-GroES system. In agreement with earlier studies, minichaperones assist folding of some proteins. However, this effect is observed only under conditions where substantial spontaneous folding is also observed and is indistinguishable from that resulting from addition of the nonchaperone protein α-casein. By contrast, the full GroE system efficiently promotes folding of several substrates under conditions where essentially no spontaneous folding is observed. These data argue that the full GroEL folding activity requires the intact GroEL-GroES complex, and in light of previous studies, underscore the importance of substrate encapsulation for providing a folding environment distinct from the bulk solution.

Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding.

The GroE proteins are molecular chaperones involved in protein folding. The general mechanism by which they facilitate folding is still enigmatic. One of the central open questions is the conformation of the GroEL-bound nonnative protein. Several suggestions have been made concerning the folding stage at which a protein can interact with GroEL. Furthermore, the possibility exists that binding of the nonnative protein to GroEL results in its unfolding. We have addressed these issues that are basic for understanding the GroE-mediated folding cycle by using folding intermediates of an Fab antibody fragment as molecular probes to define the binding properties of GroEL. We show that, in addition to binding to an early folding intermediate, GroEL is able to recognize and interact with a late quaternary-structured folding intermediate (Dc) without measurably unfolding it. Thus, the prerequisite for binding is not a certain folding stage of a nonnative protein. In contrast, general surface properties of nonnative proteins seem to be crucial for binding. Furthermore, unfolding of a highly structured intermediate does not necessarily occur upon binding to GroEL. Folding of Dc in the presence of GroEL and ATP involves cycles of binding and release. Because in this system no off-pathway reactions or kinetic traps are involved, a quantitative analysis of the reactivation kinetics observed is possible. Our results indicate that the association reaction of Dc and GroEL in the presence of ATP is rather slow, whereas in the absence of ATP association is several orders of magnitude more efficient. Therefore, it seems that ATP functions by inhibiting reassociation rather than promoting release of the bound substrate.