Characterization of wound responsive genes in Aquilaria malaccensis.

We report on the isolation and characterization of several genes responsive to wounding in the tropical endangered tree Aquilaria malaccensis. Wounding triggers the formation of a fragrant substance inside the tree stem. Deduced amino acid of the cloned sequences exhibited sequence similarities to their respective homologs: transcription factors of the WRKY gene family (AmWRKY) and β-1,3-glucanase (AmGLU). A homolog to phenylalanine ammonia-lyase (AmPAL) from previous work was also included. All cDNA sequences were of partial lengths. We studied their expression profiles in a wounding-stress experiment. Mechanical wounding induces AmWRKY in an early response to wounding (3 h), and elevates AmPAL and AmGLU expressions after 16 h. It is possible that AmWRKY mediates early wounding response while AmPAL mediates response to fungal infection by co-inducing AmGLU. Their homologs in other plants are known to inhibit fungal growth. Our data provide the first insight into the mechanisms of wounding responses in Aquilaria

Nuclear architecture and chromatin dynamics revealed by atomic force microscopy in combination with biochemistry and cell biology. Pflügers Archiv 2008

Abstract The recent technical development of atomic force microscopy (AFM) has made nano-biology of the nucleus an attractive and promising field. In this paper, we will review our current understanding of nuclear architecture and dynamics from the structural point of view. Especially, special emphases will be given to: (1) How to approach the nuclear architectures by means of new techniques using AFM, (2) the importance of the physical property of DNA in the construction of the higher-order structures, (3) the significance and implication of the linker and core histones and the nuclear matrix/scaffold proteins for the chromatin dynamics, (4) the nuclear proteins that contribute to the formation of the inner nuclear architecture. Spatio-temporal analyses using AFM, in combination with biochemical and cell biological approaches, will play important roles in the nano-biology of the nucleus, as most of nuclear structures and events occur in nanometer, piconewton and millisecond order. The new applications of AFM, such as recognition imaging, fast-scanning imaging, and a variety of modified cantilevers, are expected to be powerful techniques to reveal the nanostructure of the nucleus. Keywords Human . Cultured cells . Transport . Xenopus laevis . Regulation Architecture and biological significance of the nucleus: an overview The nucleus is the biggest organelle in eukaryotic cells (10-20 μm in a diameter in mammalian cells), and it packages the entire genome. It has long been thought that the nucleus is a container that holds nuclear events including gene duplication, transcription, and damage repair. Recent reports, however, have shown that the architecture of the nucleus itself plays important roles in the regulation of genome functions and structures. Namely, the nuclear architecture is closely related to the nuclear functions In eukaryotes, the genomic DNA is separated from the cytoplasm by the nuclear envelope and forms chromatin inside the nucleus A well-known function of the nuclear envelope is protection of the genome from environmental damage, such Pflugers Arch -Eur J Physiol (2008) 456:139-15

A unique leucine-valine adhesive motif supports structure and function of protein disulfide isomerase P5 via dimerization

P5, also known as PDIA6, is a PDI family member involved in the ER quality control. Here, we revealed that P5 dimerizes via a unique adhesive motif contained in the N-terminal thioredoxin-like domain. Unlike conventional leucine zipper motifs with leucine residues every two helical turns on ∼30-residue parallel α helices, this adhesive motif includes periodic repeats of leucine/valine residues at the third or fourth position spanning five helical turns on 15-residue anti-parallel α helices. The P5 dimerization interface is further stabilized by several reciprocal salt bridges and C-capping interactions between protomers. A monomeric P5 mutant with the impaired adhesive motif showed structural instability and local unfolding, and behaved as aberrant proteins that induce the ER stress response. Disassembly of P5 to monomers compromised its ability to inactivate IRE1α via intermolecular disulfide bond reduction and its Ca2+-dependent regulation of chaperone function in vitro. Thus, the leucine-valine adhesive motif supports structure and function of P5. © 2021 Elsevier Ltd1