Late Paleozoic geology of the Queensland Plateau (offshore northeastern Australia)

The southwestern Pacific region consists of segmented and translated continental fragments of the Gondwanan margin. Tectonic reconstructions of this region are challenged by the fact that many fragmented continental blocks are submerged and/or concealed under younger sedimentary cover. The Queensland Plateau (offshore northeastern Australia) is one such submerged continental block. We present detrital zircon geochronological and morphological data, complemented by petrographic observations, from samples obtained from the only two drill cores that penetrated the Paleozoic metasedimentary strata of the Queensland Plateau (Ocean Drilling Program leg 133, sites 824 and 825). Results provide maximum age constraints of 319.4 +/- 3.5 and 298.9 +/- 2.5 Ma for the time of deposition, which in conjunction with evidence for deformation, indicate that the metasedimentary successions are most likely upper Carboniferous to lower Permian. A comparison of our results with a larger dataset of detrital zircon ages from the Tasmanides suggests that the Paleozoic successions of the Queensland Plateau formed in a backarc basin that was part of the northern continuation of the New England Orogen and/or the East Australian Rift System. However, unlike most of the New England Orogen, a distinctive component of the detrital zircon age spectra of the Mossman Orogen is also recognised, suggesting the existence of a late Paleozoic drainage system that crossed the northern Tasmanides en route from the North Australian Craton. A distinctive shift from abraded zircon grains to grains with well-preserved morphology at ca 305 Ma reflects a direct drainage of first-cycle sediments, most likely from an outboard arc and/or backarc magmatism

Role of the Subunits Interactions in the Conformational Transitions in Adult Human Hemoglobin: an Explicit Solvent Molecular Dynamics Study

Hemoglobin exhibits allosteric structural changes upon ligand binding due to the dynamic interactions between the ligand binding sites, the amino acids residues and some other solutes present under physiological conditions. In the present study, the dynamical and quaternary structural changes occurring in two unligated (deoxy-) T structures, and two fully ligated (oxy-) R, R2 structures of adult human hemoglobin were investigated with molecular dynamics. It is shown that, in the sub-microsecond time scale, there is no marked difference in the global dynamics of the amino acids residues in both the oxy- and the deoxy- forms of the individual structures. In addition, the R, R2 are relatively stable and do not present quaternary conformational changes within the time scale of our simulations while the T structure is dynamically more flexible and exhibited the T\rightarrow R quaternary conformational transition, which is propagated by the relative rotation of the residues at the {\alpha}1{\beta}2 and {\alpha}2{\beta}1 interface.Comment: Reprinted (adapted) with permission from J. Phys. Chem. B DOI:10.1021/jp3022908. Copyright (2012) American Chemical Societ

Introducing standardized field methods for fracture-focused surface process research

Rock fractures are a key contributor to a broad array of Earth surface processes due to their direct control on rock strength as well as rock porosity and permeability. However, to date, there has been no standardization for the quantification of rock fractures in surface process research. In this work, the case is made for standardization within fracture-focused research, and prior work is reviewed to identify various key datasets and methodologies. Then, a suite of standardized methods is presented as a starting “baseline” for fracture-based research in surface process studies. These methods have been shown in pre-existing work from structural geology, geotechnical engineering, and surface process disciplines to comprise best practices for the characterization of fractures in clasts and outcrops. This practical, accessible, and detailed guide can be readily employed across all fracture-focused weathering and geomorphology applications. The wide adoption of a baseline of data collected using the same methods will enable comparison and compilation of datasets among studies globally and will ultimately lead to a better understanding of the links and feedbacks between rock fracture and landscape evolution.</p

Mycobacterium tuberculosis Rv3586 (DacA) Is a Diadenylate Cyclase That Converts ATP or ADP into c-di-AMP

Cyclic diguanosine monophosphate (c-di-GMP) and cyclic diadenosine monophosphate (c-di-AMP) are recently identified signaling molecules. c-di-GMP has been shown to play important roles in bacterial pathogenesis, whereas information about c-di-AMP remains very limited. Mycobacterium tuberculosis Rv3586 (DacA), which is an ortholog of Bacillus subtilis DisA, is a putative diadenylate cyclase. In this study, we determined the enzymatic activity of DacA in vitro using high-performance liquid chromatography (HPLC), mass spectrometry (MS) and thin layer chromatography (TLC). Our results showed that DacA was mainly a diadenylate cyclase, which resembles DisA. In addition, DacA also exhibited residual ATPase and ADPase in vitro. Among the potential substrates tested, DacA was able to utilize both ATP and ADP, but not AMP, pApA, c-di-AMP or GTP. By using gel filtration and analytical ultracentrifugation, we further demonstrated that DacA existed as an octamer, with the N-terminal domain contributing to tetramerization and the C-terminal domain providing additional dimerization. Both the N-terminal and the C-terminal domains were essential for the DacA's enzymatically active conformation. The diadenylate cyclase activity of DacA was dependent on divalent metal ions such as Mg2+, Mn2+ or Co2+. DacA was more active at a basic pH rather than at an acidic pH. The conserved RHR motif in DacA was essential for interacting with ATP, and mutation of this motif to AAA completely abolished DacA's diadenylate cyclase activity. These results provide the molecular basis for designating DacA as a diadenylate cyclase. Our future studies will explore the biological function of this enzyme in M. tuberculosis

c-di-AMP Is a New Second Messenger in Staphylococcus aureus with a Role in Controlling Cell Size and Envelope Stress.

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