<Poster Presentation 3>Covariant Lyapunov Analysis of Chaotic Kolmogorov Flows and Time-correlation Function

[Date] November 28 (Mon) - December 2 (Fri), 2011: [Place] Kyoto University Clock Tower Centennial Hall, Kyoto, JAPA

Inositol Acylation of Phosphatidylinositol Mannosides: A Rapid Mass Response to Membrane Fluidization in Mycobacteria

Mycobacteria share an unusually complex, multilayered cell envelope, which contributes to adaptation to changing environments. The plasma membrane is the deepest layer of the cell envelope and acts as the final permeability barrier against outside molecules. There is an obvious need to maintain the plasma membrane integrity, but the adaptive responses of the plasma membrane to stress exposure remain poorly understood. Using chemical treatment and heat stress to fluidize the membrane, we show here that phosphatidylinositol (PI)-anchored plasma membrane glycolipids known as PI mannosides (PIMs) are rapidly remodeled upon membrane fluidization in Mycobacterium smegmatis. Without membrane stress, PIMs are predominantly in a triacylated form: two acyl chains of the PI moiety plus one acyl chain modified at one of the mannose residues. Upon membrane fluidization, we determined the fourth fatty acid is added to the inositol moiety of PIMs, making them tetra-acylated variants. Additionally, we show that PIM inositol acylation is a rapid response independent of de novo protein synthesis, representing one of the fastest mass conversions of lipid molecules found in nature. Strikingly, we found that M. smegmatis is more resistant to the bactericidal effect of a cationic detergent after benzyl alcohol pre-exposure. We further demonstrate that fluidization-induced PIM inositol acylation is conserved in pathogens such as Mycobacterium tuberculosis and Mycobacterium abscessus. Our results demonstrate that mycobacteria possess a mechanism to sense plasma membrane fluidity change. We suggest that inositol acylation of PIMs is a novel membrane stress response that enables mycobacterial cells to resist membrane fluidization

Chaos-assisted emission from asymmetric resonant cavity microlasers

We study emission from quasi-one-dimensional modes of an asymmetric resonant cavity that are associated with a stable periodic ray orbit confined inside the cavity by total internal reflection. It is numerically demonstrated that such modes exhibit directional emission, which is explained by chaos-assisted emission induced by dynamical tunneling. Fabricating semiconductor microlasers with the asymmetric resonant cavity, we experimentally demonstrate the selective excitation of the quasi-one-dimensional modes by employing the device structure to preferentially inject currents to these modes and observe directional emission in good accordance with the theoretical prediction based on chaos-assisted emission.Comment: 9 pages, 10 figures, some figures are in reduced qualit

The circulation pattern and day-night heat transport in the atmosphere of a synchronously rotating aquaplanet: Dependence on planetary rotation rate

In order to investigate a possible variety of atmospheric states realized on a synchronously rotating aquaplanet, an experiment studying the impact of planetary rotation rate is performed using an atmospheric general circulation model (GCM) with simplified hydrological and radiative processes. The entire planetary surface is covered with a swamp ocean. The value of planetary rotation rate is varied from zero to the Earth’s, while other parameters such as planetary radius, mean molecular weight and total mass of atmospheric dry components, and solar constant are set to the present Earth’s values. The integration results show that the atmosphere reaches statistically equilibrium states for all runs; none of the calculated cases exemplifies the runaway greenhouse state. The circulation patterns obtained are classified into four types: Type-I characterized by the dominance of a day-night thermally direct circulation, Type-II characterized by a zonal wave number one resonant Rossby wave over a meridionally broad westerly jet on the equator, Type-III characterized by a long time scale north-south asymmetric variation, and Type-IV characterized by a pair of mid-latitude westerly jets. With the increase of planetary rotation rate, the circulation evolves from Type-I to Type-II and then to Type-III gradually and smoothly, whereas the change from Type-III to Type-IV is abrupt and discontinuous. Over a finite range of planetary rotation rate, both Types-III and -IV emerge as statistically steady states, constituting multiple equilibria. In spite of the substantial changes in circulation, the net energy transport from the day side to the night side remains almost insensitive to planetary rotation rate, although the partition into dry static energy and latent heat energy transports changes. The reason for this notable insensitivity is that the outgoing longwave radiation over the broad area of the day side is constrained by the radiation limit of a moist atmosphere, so that the transport to the night side, which is determined as the difference between the incoming solar radiation and the radiation limit, cannot change greatly

Cell wall damage reveals spatial flexibility in peptidoglycan synthesis and a non-redundant role for RodA in mycobacteria [preprint]

Cell wall peptidoglycan is a heteropolymeric mesh that protects the bacteria from internal turgor and external insults. In many rod-shaped bacteria, peptidoglycan synthesis for normal growth is achieved by two distinct pathways: the Rod complex, comprised of MreB, RodA and a cognate class B PBP, and the class A PBPs. In contrast to laterally-growing bacteria, pole-growing mycobacteria do not encode an MreB homolog and do not require SEDS protein RodA for in vitro growth. However, RodA contributes to survival of Mycobacterium tuberculosis in some infection models, suggesting that the protein could have a stress-dependent role in maintaining cell wall integrity. Under basal conditions, we find here that the subcellular distribution of RodA largely overlaps with that of the aPBP PonA1, and that both RodA and the aPBPs promote polar peptidoglycan assembly. Upon cell wall damage, RodA fortifies M. smegmatis against lysis and, unlike aPBPs, contributes to a shift in peptidoglycan assembly from the poles to the sidewall. Neither RodA nor PonA1 relocalize; instead, the redistribution of nascent cell wall parallels that of peptidoglycan precursor synthase MurG. Our results support a model in which mycobacteria balance polar growth and cell-wide repair via spatial flexibility in precursor synthesis and extracellular insertion. Importance Peptidoglycan synthesis is a highly successful target for antibiotics. The pathway has been extensively studied in model organisms under laboratory-optimized conditions. In natural environments, bacteria are frequently under attack. Moreover the vast majority of bacterial species are unlikely to fit a single paradigm because of differences in growth mode and/or envelope structure. Studying cell wall synthesis under non-optimal conditions and in non-standard species may improve our understanding of pathway function and suggest new inhibition strategies. Mycobacterium smegmatis, a relative of several notorious human and animal pathogens, has an unusual polar growth mode and multi-layered envelope. In this work we challenged M. smegmatis with cell wall-damaging enzymes to characterize the roles of cell wall-building enzymes when the bacterium is under attack

The MYB36 transcription factor orchestrates Casparian strip formation

The endodermis in roots acts as a selectivity filter for nutrient and water transport essential for growth and development. This selectivity is enabled by the formation of lignin-based Casparian strips. Casparian strip formation is initiated by the localization of the Casparian strip domain proteins (CASPs) in the plasma membrane, at the site where the Casparian strip will form. Localized CASPs recruit Peroxidase 64 (PER64), a Respiratory Burst Oxidase Homolog F, and Enhanced Suberin 1 (ESB1), a dirigent-like protein, to assemble the lignin polymerization machinery. However, the factors that control both expression of the genes encoding this biosynthetic machinery and its localization to the Casparian strip formation site remain unknown. Here, we identify the transcription factor, MYB36, essential for Casparian strip formation. MYB36 directly and positively regulates the expression of the Casparian strip genes CASP1, PER64, and ESB1. Casparian strips are absent in plants lacking a functional MYB36 and are replaced by ectopic lignin-like material in the corners of endodermal cells. The barrier function of Casparian strips in these plants is also disrupted. Significantly, ectopic expression of MYB36 in the cortex is sufficient to reprogram these cells to start expressing CASP1–GFP, correctly localize the CASP1–GFP protein to form a Casparian strip domain, and deposit a Casparian strip-like structure in the cell wall at this location. These results demonstrate that MYB36 is controlling expression of the machinery required to locally polymerize lignin in a fine band in the cell wall for the formation of the Casparian strip