Lower Kimmeridgian layer with bored and encrusted hiatus concretions (Upper Jurassic, Central Poland) : implications for stratigraphy and basin evolution

The paper presents a comparative analysis of a Lower Kimmeridgian layer with bored and encrusted hiatus concretions collected in three study areas, located in Central Poland. These studies demonstrate distinct similarities between the hiatus concretions in terms of their origin, development and stratigraphic position. The layer with its characteristic concretions seems to represent an important marker horizon for the Lower Kimmeridgian successions in Central Poland. The identification of this marker horizon in drill cores and exposures could be important for definition of the stratigraphic position of the sediments, which otherwise lack appropriate biostratigraphic information. The matrix of the concretions is composed of pelagic calciturbidites, which reflect flooding of the early Kimmeridgian platform. These sediments were lithified early and formed a hardground. The origin of the hiatus concretions probably is related to erosion of the hardground, followed by redeposition and several phases of exhumation and erosion, preceding final burial. The characteristic ecological successions, observed in the concretions, document an evolution from soft to firm and hard marine substrates, typical of hardgrounds and evidenced by various burrows, borings (Gastrochaenolites, Trypanites), and epizoans. Calciturbidite sedimentation, hardground erosion and redeposition of the hiatus concretions, known from deposits of the Platynota Zone in Central Poland, were associated with synsedimentary activity of the Holy Cross Fault, on the NE margin of the extensive, tectonic Małopolska Block

Sedimentary successions in the Middle-Upper Oxfordian reef deposits from the southern part of the Kraków-Częstochowa Upland (Southern Poland)

The sedimentary succession of the largest example of an Upper Oxfordian reef located in the southern part of the Polish sector of the northern Tethys shelf is described. Detailed sampling of exposures enabled characterization of the full succession of facies and microfacies diversity, documenting the reef evolution. The succession studied represents the maximum development of Upper Jurassic reefs in Poland corresponding to the upper Transversarium and the Bifurcatus zones, and followed by drowning of the carbonate platform in the lower Bimmamatum Zone. The reef succession comprises three types of facies, in which eight important microfacies types were distingushed, reflecting several stages of reef development. Mid-ramp, microbial-sponge frame-reefs represent a transgressive depositional sequence, up to tens of metres thick. A microbial-Crescentiella-ooid and ooid-intraclast-bioclast facies form numerous, decimetre- to metre-scale, sequences corresponding to higher-order, transgressive/regressive sea level changes. These facies represent a mid-inner ramp setting when sedimentation was dominated by bioclasts and non-skeletal grains (mainly ooids, oncoids, aggregate grains and intraclasts). The grains were stabilized by microbialites and cemented in early diagenesis, which created grain-dominated, microbial-cement supported reefs. As a result, both the mid-ramp, microbial-sponge frame-reefs and the shallow-water, grain-dominated, microbial-cement supported reefs form extensive, strongly lithified Oxfordian reef complexes in the Kraków-Częstochowa Upland

The crystal and solution studies of glucosamine-6-phosphate synthase from Candida albicans.

Glucosamine 6-phosphate (GlcN-6-P) synthase is an ubiquitous enzyme that catalyses the first committed step in the reaction pathway that leads to formation of uridine 5'-diphospho-N-acetyl-D-glucosamine (UDP-GlcNAc), a precursor of macromolecules that contain amino sugars. Despite sequence similarities, the enzyme in eukaryotes is tetrameric, whereas in prokaryotes it is a dimer. The activity of eukaryotic GlcN-6-P synthase (known as Gfa1p) is regulated by feedback inhibition by UDP-GlcNAc, the end product of the reaction pathway, whereas in prokaryotes the GlcN-6-P synthase (known as GlmS) is not regulated at the post-translational level. In bacteria and fungi the enzyme is essential for cell wall synthesis. In human the enzyme is a mediator of insulin resistance. For these reasons, Gfa1p is a target in anti-fungal chemotherapy and in therapeutics for type-2 diabetes. The crystal structure of the Gfa1p isomerase domain from Candida albicans has been analysed in complex with the allosteric inhibitor UDP-GlcNAc and in the presence of glucose 6-phosphate, fructose 6-phosphate and an analogue of the reaction intermediate, 2-amino-2-deoxy-d-mannitol 6-phosphate (ADMP). A solution structure of the native Gfa1p has been deduced using small-angle X-ray scattering (SAXS). The tetrameric Gfa1p can be described as a dimer of dimers, with each half similar to the related enzyme from Escherichia coli. The core of the protein consists of the isomerase domains. UDP-GlcNAc binds, together with a metal cation, in a well-defined pocket on the surface of the isomerase domain. The residues responsible for tetramerisation and for binding UDP-GlcNAc are conserved only among eukaryotic sequences. Comparison with the previously studied GlmS from E. coli reveals differences as well as similarities in the isomerase active site. This study of Gfa1p focuses on the features that distinguish it from the prokaryotic homologue in terms of quaternary structure, control of the enzymatic activity and details of the isomerase active site