The role of cysteine in the formation of domain structures of papain and legumin in peas, involved in limited proteolysis

The limited use of plant proteins for food is explained by their low bioavailability and poor digestibility by enzymes of the gastrointestinal tract. Partially reproduced enzymatic processes of limited proteolysis that occur during seed germination are used to modify and improve the edibility characteristics of seed proteins. The present work discusses the possibility of reducing the duration of seed germination processes by optimising the conditions and parameters of limited proteolysis. To optimise manufacturing high-quality final product, enzymes (additional to the natural enzymes in the seed) and proteolysis conditions (in this case, temperature), as well as added substances (hydrolysis activators), were selected. The influence of cysteine on the formation of domain structures of proteins (enzymes and globulins) was evaluated. The proposed expressions can be used to determine those fragments of protein molecules that form stable domains and become unstructured when exposed to enzymes. Optimal conditions for limited proteolysis were identified based on the physical mechanism of action of papain-like proteolytic enzymes on pea legumin LegA (3KSC, CAA10722). It is shown that the decomposition of protein secondary structures takes 6–8 times longer, since the formed hydrogen bonds limit the access of enzymes to the corresponding amino-acid residues. It is also demonstrated that the decomposition of hydrogen bonds, e.g. by preliminary heat treatment of proteins, will broaden the prospects for limited proteolysis.

Probing the Nanoscale Heterogeneous Mixing in a High-Performance Polymer Blend

The blend of polyetheretherketone (PEEK) and polybenzimidazole (PBI) produces a high-performance blend (PPB) that is a potential replacement material in several industries due to its high temperature stability and desirable tribological properties. Understanding the nanoscale structure and interface of the two domains of the blend is critical for elucidating the origin of these desirable properties. Whilst achieving the physical characterisation of the domain structures is relatively uncomplicated, the elucidation of structures at the interface presents a significant experimental challenge. In this work, we combine atomic force microscopy (AFM) with an IR laser (AFM-IR) and thermal cantilever probes (nanoTA) to gain insights into the chemical heterogeneity and extent of mixing within the blend structure for the first time. The AFM-IR and nanoTA measurements show that domains in the blend are compositionally different from those of the pure PEEK and PBI polymers, with significant variations observed in a transition region several microns wide in proximity to domain boundary. This strongly points to physical mixing of the two components on a molecular scale at the interface. The versatility intrinsic to the combined methodology employed in this work provides nano- and microscale chemical information that can be used to understand the link between properties of different length scales across a wide range of materials.

Pregnancy-specific glycoproteins: evolution, expression, functions, and disease associations.

Pregnancy-specific glycoproteins (PSGs) are members of the immunoglobulin superfamily and are closely related to the predominantly membrane-bound CEACAM proteins. PSGs are produced by placental trophoblasts and secreted into the maternal bloodstream at high levels where they may regulate maternal immune and vascular functions through receptor binding and modulation of cytokine and chemokine expression and activity. PSGs may have autocrine and paracrine functions in the placental bed, and PSGs can activate soluble and extracellular matrix bound TGF-β, with potentially diverse effects on multiple cell types. PSGs are also found at high levels in the maternal circulation, at least in human, where they may have endocrine functions. In a non-reproductive context, PSGs are expressed in the gastrointestinal tract and their deregulation may be associated with colorectal cancer and other diseases. Like many placental hormones, PSGs are encoded by multigene families and they have an unusual phylogenetic distribution, being found predominantly in species with hemochorial placentation, with the notable exception of the horse in which PSG-like proteins are expressed in the endometrial cups of the epitheliochorial placenta. The evolution and expansion of PSG gene families appears to be a highly active process, with significant changes in gene numbers and protein domain structures in different mammalian lineages, and reports of extensive copy number variation at the human locus. Against this apparent diversification, the available evidence indicates extensive conservation of PSG functions in multiple species. These observations are consistent with maternal-fetal conflict underpinning the evolution of PSGs.

Magnetic State Switching in FeGa Microstructures

This work demonstrates that magnetoelectric composite heterostructures can be designed at the length scale of 10 microns that can be switched from a magnetized state to a vortex state, effectively switching the magnetization off, using electric field induced strain. This was accomplished using thin film magnetoelectric heterostructures of Fe81.4Ga18.6 on a single crystal (011) [Pb(Mg1/3Nb2/3)O3]0.68-[PbTiO3]0.32 (PMN-32PT) ferroelectric substrate. The heterostructures were tripped from a multi-domain magnetized state to a flux closure vortex state using voltage induced strain in a piezoelectric substrate. FeGa heterostructures were deposited on a Si-substrate for SQUID magnetometry characterization of the magnetic properties. The magnetoelectric coupling of a FeGa continuous film on PMN-32PT was characterized using a MOKE magnetometer with bi-axial strain gauges, and magnetic multi-domain heterostructures were imaged using X-Ray Magnetic Circular Dichroism – Photoemission Electron Microscopy (XMCD-PEEM) during the transition to the vortex state. The domain structures were modelled using MuMax3, a micromagnetics code, and compared with observations. The results provide considerable insight into designing magnetoelectric heterostructures that can be switched from an “on” state to an “off” state using electric field induced strain.

Temperature Dependence of Dielectric Properties of Ferroelectric Heterostructures with Domain-Provided Negative Capacitance

It is well known that the ferroelectric layers in dielectric/ferroelectric/dielectric heterostructures harbor polarization domains resulting in the negative capacitance crucial for manufacturing energy-efficient field-effect transistors. However, the temperature behavior of the characteristic dielectric properties, and, hence, the corresponding behavior of the negative capacitance, are still poorly understood, restraining the technological progress thereof. Here we investigate the temperature-dependent properties of domain structures in the SrTiO3/PbTiO3/SrTiO3 heterostructures and demonstrate that the temperature–thickness phase diagram of the system includes the ferroelectric and paraelectric regions, which exhibit different responses to the applied electric field. Using phase-field modeling and analytical calculations we find the temperature dependence of the dielectric constant of ferroelectric layers and identify the regions of the phase diagram wherein the system demonstrates negative capacitance. We further discuss the optimal routes for implementing negative capacitance in energy-efficient ferroelectric field-effect transistors.

Deepening of domains at e-beam writing on the -Z surface of lithium niobate

The focus of the study was to investigate the peculiarities of the domains created by electron beam (e-beam) in a surface layer of congruent lithium niobate, which comparable to a depth of electron beam charge penetration. Direct e-beam writing (DEBW) of different domain structures with a scanning electron microscope was performed on the polar -Z cut. Accelerating voltage 15 kV and e-beam current 100 pA were applied. Different patterns of local irradiated squares were used to create domain structures and single domains. No domain contrast was observed by the PFM technique. Based on chemical etching, it was found that the vertices of the domains created do not reach the surface level. The average deepening of the domain vertices was several hundred nanometers and varied depending on the irradiation dose and the location of the irradiated areas (squares) relative to each other. Computer simulation was applied to analyze the spatial distribution of the electric field in the various irradiated patterns. The deepening was explained by the fact that in the near-surface layer there is a sign inversion of the normal component of the electric field strength vector, which controls the domain formation during DEBW. Thus, with the help of e-beam, domains were created completely located in the bulk, in contrast to the domains that are nucleated on the surface of the -Z cut during the polarization inversion with AFM tip. The detected deepening of e-beam domains suggests the possibility of creating the “head-to-head” domain walls in the near-surface layer lithium niobate by DEBW.

Comprehensive Analysis of Jumonji Domain C Family from Citrus grandis and Expression Profilings in the Exocarps of “Huajuhong” (Citrus grandis “Tomentosa”) during Various Development Stages

Citrus grandis “Tomentosa” (“Huajuhong”) is a famous Traditional Chinese Medicine. In this study, a total of 18 jumonji C (JMJC) domain-containing proteins were identified from C. grandis. The 18 CgJMJCs were unevenly located on six chromosomes of C. grandis. Phylogenetic analysis revealed that they could be classified into five groups, namely KDM3, KDM4, KDM5, JMJC, and JMJD6. The domain structures and motif architectures in the five groups were diversified. Cis-acting elements on the promoters of 18 CgJMJC genes were also investigated, and the abscisic acid-responsive element (ABRE) was distributed on 15 CgJMJC genes. Furthermore, the expression profiles of 18 CgJMJCs members in the exocarps of three varieties of “Huajuhong”, for different developmental stages, were examined. The results were validated by quantitative real-time PCR (qRT-PCR). The present study provides a comprehensive characterization of JMJC domain-containing proteins in C. grandis and their expression patterns in the exocarps of C. grandis “Tomentosa” for three varieties with various development stages.

Phylogenetic Analysis of Canonical/non-canonical Dicers and RNase III Containing Proteins in Fungal Kingdom

Background: Dicers were member of RNase III containing proteins family with important RNAi function in eukaryotes. In this study, we tried to address the potential distribution of all RNase III containing proteins among the fungal kingdom, as well as their possible evolution paths including canonical Dicers, non-canonical Dicers and non-canonical Dicer-like proteins.Result: RNase III containing proteins were collected from 83 species, and discussed the features and possible evolution pathways of RNase III containing protein family. In general, RNase III containing protein family could be characterized into three different groups as canonical Dicer, non-canonical Dicers and Dicer-like proteins based on their domain structures and functional annotation. Most eukaryotes obtained multiple RNase III protein of different types at the same time, including canonical Dicers and Dicer-like proteins. Phylogenetic analysis showed that the RNase III domains were different between canonical Dicers and Dicer-like proteins, for the first and second RNase III domains had different insertions in different regions with certain extent of conservation. Regardless of the types, RNA-binging domains in RNase III protein family were very similar to each other. Furthermore, short insertions were found in different positions from the first and second RNase III domains in canonical Dicers separately. RNA-binging domains from all types were quite similar to each other.Conclusion: RNase III containing proteins in general widely exist in eukaryotes with minor divergent among different types and groups. Suggested by the RNase III and RDB domains, the canonical/non-canonical Dicers Dicer-like proteins might share the same ancestor and have evolved from separate mild-types through different directions.

MORC protein family-related signature within human disease and cancer

The microrchidia (MORC) family of proteins is a highly conserved nuclear protein superfamily, whose members contain common domain structures (GHKL-ATPase, CW-type zinc finger and coiled-coil domain) yet exhibit diverse biological functions. Despite the advancing research in previous decades, much of which focuses on their role as epigenetic regulators and in chromatin remodeling, relatively little is known about the role of MORCs in tumorigenesis and pathogenesis. MORCs were first identified as epigenetic regulators and chromatin remodelers in germ cell development. Currently, MORCs are regarded as disease genes that are involved in various human disorders and oncogenes in cancer progression and are expected to be the important biomarkers for diagnosis and treatment. A new paradigm of expanded MORC family function has raised questions regarding the regulation of MORCs and their biological role at the subcellular level. Here, we systematically review the progress of researching MORC members with respect to their domain architectures, diverse biological functions, and distribution characteristics and discuss the emerging roles of the aberrant expression or mutation of MORC family members in human disorders and cancer development. Furthermore, the illustration of related mechanisms of the MORC family has made MORCs promising targets for developing diagnostic tools and therapeutic treatments for human diseases, including cancers.