Age Sequence in Small Clusters Associated with Bright-Rimmed Clouds

Bright-rimmed clouds (BRCs) found in H II regions are probable sites of triggered star formation due to compression by ionization/shock fronts, and it is hypothesized that star formation proceeds from the exciting star(s) side outward of the HII region ("small-scale sequential star formation"). In order to quantitatively testify this hypothesis we undertook BVIc photometry of four BRC aggregates. The amounts of interstellar extinction and reddening for each star have been estimated by using the JHKs photometry. Then we constructed reddening-corrected V/V-Ic color-magnitude diagrams, where the age of each star has been derived. All the stars turned out to be a few tenths to a few Myr old. Although the scatters are large and the numbers of the sample stars are small, we found a clear trend that the stars inside or in the immediate vicinity of the bright rim are younger than those outside it in all the four aggregates, confirming the hypothesis in question.Comment: 10 pages, 2 figures; accepted for publication in PAS

National Physical Laboratory demonstrates 1 g Kibble balance: Linkage of macroscopic mass to Planck constant

Mass is the only base unit, which is represented as a primary standard in the form of artifact for more than 125 years. International prototype of kilogram (IPK) is kept at the Bureau International des Poids et Mesures (BIPM), Paris and serves as the international standard of kilogram. It is made of 90% platinum and 10% iridium and as a cylinder of 39 mm diameter and 39 mm height. Replicas of the IPK are made of the same material and used at BIPM as reference or working standards and national prototype of kilogram (NPK), kept at different National Metrology Institutes (NMIs). NPK-57, kept at CSIR-National Physical Laboratory, is sent periodically to BIPM for calibration

A Hydrolase of Trehalose Dimycolate Induces Nutrient Influx and Stress Sensitivity to Balance Intracellular Growth of Mycobacterium tuberculosis

SummaryChronic tuberculosis in an immunocompetent host is a consequence of the delicately balanced growth of Mycobacterium tuberculosis (Mtb) in the face of host defense mechanisms. We identify an Mtb enzyme (TdmhMtb) that hydrolyzes the mycobacterial glycolipid trehalose dimycolate and plays a critical role in balancing the intracellular growth of the pathogen. TdmhMtb is induced under nutrient-limiting conditions and remodels the Mtb envelope to increase nutrient influx but concomitantly sensitizes Mtb to stresses encountered in the host. Consistent with this, a ΔtdmhMtb mutant is more resilient to stress and grows to levels higher than those of wild-type in immunocompetent mice. By contrast, mutant growth is retarded in MyD88−/− mice, indicating that TdmhMtb provides a growth advantage to intracellular Mtb in an immunocompromised host. Thus, the effects and countereffects of TdmhMtb play an important role in balancing intracellular growth of Mtb in a manner that is directly responsive to host innate immunity

Growth of Mycobacterium tuberculosis biofilms containing free mycolic acids and harbouring drug-tolerant bacteria

Successful treatment of human tuberculosis requires 6–9 months' therapy with multiple antibiotics. Incomplete clearance of tubercle bacilli frequently results in disease relapse, presumably as a result of reactivation of persistent drug-tolerant Mycobacterium tuberculosis cells, although the nature and location of these persisters are not known. In other pathogens, antibiotic tolerance is often associated with the formation of biofilms – organized communities of surface-attached cells – but physiologically and genetically defined M. tuberculosis biofilms have not been described. Here, we show that M. tuberculosis forms biofilms with specific environmental and genetic requirements distinct from those for planktonic growth, which contain an extracellular matrix rich in free mycolic acids, and harbour an important drug-tolerant population that persist despite exposure to high levels of antibiotics

Starvation sensing by mycobacterial RelA/SpoT homologue through constitutive surveillance of translation

The stringent response, which leads to persistence of nutrient-starved mycobacteria, is induced by activation of the RelA/SpoT homolog (Rsh) upon entry of a deacylated-tRNA in a translating ribosome. However, the mechanism by which Rsh identifies such ribosomes in vivo remains unclear. Here, we show that conditions inducing ribosome hibernation result in loss of intracellular Rsh in a Clp protease-dependent manner. This loss is also observed in nonstarved cells using mutations in Rsh that block its interaction with the ribosome, indicating that Rsh association with the ribosome is important for Rsh stability. The cryo-EM structure of the Rsh-bound 70S ribosome in a translation initiation complex reveals unknown interactions between the ACT domain of Rsh and components of the ribosomal L7/L12 stalk base, suggesting that the aminoacylation status of A-site tRNA is surveilled during the first cycle of elongation. Altogether, we propose a surveillance model of Rsh activation that originates from its constitutive interaction with the ribosomes entering the translation cycle

Unveiling the Importance of Magnetic Fields in the Evolution of Dense Clumps Formed at the Waist of Bipolar H ii Regions: A Case Study of Sh 2-201 with JCMT SCUBA-2/POL-2

Abstract: We present the properties of magnetic fields (B fields) in two clumps (clump 1 and clump 2), located at the waist of the bipolar H ii region Sh 2-201, based on James Clerk Maxwell Telescope SCUBA-2/POL-2 observations of 850 μm polarized dust emission. We find that B fields in the direction of the clumps are bent and compressed, showing bow-like morphologies, which we attribute to the feedback effect of the H ii region on the surface of the clumps. Using the modified Davis–Chandrasekhar–Fermi method, we estimate B-field strengths of 266 and 65 μG for clump 1 and clump 2, respectively. From virial analyses and critical mass ratio estimates, we argue that clump 1 is gravitationally bound and could be undergoing collapse, whereas clump 2 is unbound and stable. We hypothesize that the interplay of the thermal pressure imparted by the H ii region, the B-field morphologies, and the various internal pressures of the clumps (such as magnetic, turbulent, and gas thermal pressures) has the following consequences: (a) formation of clumps at the waist of the H ii region; (b) progressive compression and enhancement of the B fields in the clumps; (c) stronger B fields that will shield the clumps from erosion by the H ii region and cause pressure equilibrium between the clumps and the H ii region, thereby allowing expanding ionization fronts to blow away from the filament ridge, forming bipolar H ii regions; and (d) stronger B fields and turbulence that will be able to stabilize the clumps. A study of a larger sample of bipolar H ii regions would help to determine whether our hypotheses are widely applicable

Starvation Sensing by Mycobacterial RelA/SpoT Homologue Through Constitutive Surveillance of Translation

The stringent response, which leads to persistence of nutrient-starved mycobacteria, is induced by activation of the RelA/SpoT homolog (Rsh) upon entry of a deacylated-tRNA in a translating ribosome. However, the mechanism by which Rsh identifies such ribosomes in vivo remains unclear. Here, we show that conditions inducing ribosome hibernation result in loss of intracellular Rsh in a Clp protease-dependent manner. This loss is also observed in nonstarved cells using mutations in Rsh that block its interaction with the ribosome, indicating that Rsh association with the ribosome is important for Rsh stability. The cryo-EM structure of the Rsh-bound 70S ribosome in a translation initiation complex reveals unknown interactions between the ACT domain of Rsh and components of the ribosomal L7/L12 stalk base, suggesting that the aminoacylation status of A-site tRNA is surveilled during the first cycle of elongation. Altogether, we propose a surveillance model of Rsh activation that originates from its constitutive interaction with the ribosomes entering the translation cycle