Lyman Break Galaxies at z∼5z\sim5: Rest-Frame UV Spectra

We report initial results for spectroscopic observations of candidates of Lyman Break Galaxies (LBGs) at $z\sim5$ in a region centered on the Hubble Deep Field-North by using the Faint Object Camera and Spectrograph attached to the Subaru Telescope. Eight objects with $I_C\leq25.0$ mag, including one AGN, are confirmed to be at $4.5<z<5.2$. The rest-frame UV spectra of seven LBGs commonly show no or weak Lyalpha emission line (rest-frame equivalent width of 0-10\AA) and relatively strong low-ionization interstellar metal absorption lines of SiII $\lambda$1260, OI+SiII $\lambda$1303, and CII $\lambda$1334 (mean rest-frame equivalent widths of them are $-1.2 \sim -5.1$\AA). These properties are significantly different from those of the mean rest-frame UV spectrum of LBGs at $z\sim3$, but are quite similar to those of subgroups of LBGs at $z\sim3$ with no or weak Lyalpha emission. The weakness of Lyalpha emission and strong low-ionization interstellar metal absorption lines may indicate that these LBGs at $z\sim5$ are chemically evolved to some degree and have a dusty environment. Since the fraction of such LBGs at $z\sim5$ in our sample is larger than that at $z\sim3$, we may witness some sign of evolution of LBGs from $z\sim5$ to $z\sim3$, though the present sample size is very small. It is also possible, however, that the brighter LBGs tend to show no or weak Lyalpha emission, because our spectroscopic sample is bright (brighter than $L^{\ast}$) among LBGs at $z\sim5$. More observations are required to establish spectroscopic nature of LBGs at $z\sim5$.Comment: 16 pages, 3 figures, accepted by Ap

High-resolution cryo-EM structure of photosystem II reveals damage from high-dose electron beams

Photosystem II (PSII) plays a key role in water-splitting and oxygen evolution. X-ray crystallography has revealed its atomic structure and some intermediate structures. However, these structures are in the crystalline state and its final state structure has not been solved. Here we analyzed the structure of PSII in solution at 1.95 Å resolution by single-particle cryo-electron microscopy (cryo-EM). The structure obtained is similar to the crystal structure, but a PsbY subunit was visible in the cryo-EM structure, indicating that it represents its physiological state more closely. Electron beam damage was observed at a high-dose in the regions that were easily affected by redox states, and reducing the beam dosage by reducing frames from 50 to 2 yielded a similar resolution but reduced the damage remarkably. This study will serve as a good indicator for determining damage-free cryo-EM structures of not only PSII but also all biological samples, especially redox-active metalloproteins

ICTV Virus Taxonomy Profile: Megabirnaviridae

Megabirnaviridae is a family of non-enveloped spherical viruses with dsRNA genomes of two linear segments, each of 7.2-8.9 kbp, comprising 16.1 kbp in total. The genus Megabirnavirus includes the species Rosellinia necatrix megabirnavirus 1, the exemplar isolate of which infects the white root rot fungus (Rosellinia necatrix) to which it confers hypovirulence. Megabirnaviruses are characterized by their bisegmented genome with large 5'-untranslated regions (1.6 kb) upstream of both 5'-proximal coding strand ORFs, and large protrusions on the particle surface. This is a summary of the ICTV Report on the family Megabirnaviridae, which is available at ictv.global/report/megabirnaviridae

Structure of a tetrameric photosystem I from a glaucophyte alga Cyanophora paradoxa

Photosystem I (PSI) is one of the two photosystems functioning in light-energy harvesting, transfer, and electron transfer in photosynthesis. However, the oligomerization state of PSI is variable among photosynthetic organisms. We present a 3.8-angstrom resolution cryo-electron microscopic structure of tetrameric PSI isolated from the glaucophyte alga Cyanophora paradoxa, which reveals differences with PSI from other organisms in subunit composition and organization. The PSI tetramer is organized in a dimer of dimers with a C2 symmetry. Unlike cyanobacterial PSI tetramers, two of the four monomers are rotated around 90 degrees, resulting in a completely different pattern of monomer-monomer interactions. Excitation-energy transfer among chlorophylls differs significantly between Cyanophora and cyanobacterial PSI tetramers. These structural and spectroscopic features reveal characteristic interactions and excitation-energy transfer in the Cyanophora PSI tetramer, suggesting that the Cyanophora PSI could represent a turning point in the evolution of PSI from prokaryotes to eukaryotes

Structures of the wild-type MexAB–OprM tripartite pump reveal its complex formation and drug efflux mechanism

In Pseudomonas aeruginosa, MexAB–OprM plays a central role in multidrug resistance by ejecting various drug compounds, which is one of the causes of serious nosocomial infections. Although the structures of the components of MexAB–OprM have been solved individually by X-ray crystallography, no structural information for fully assembled pumps from P. aeruginosa were previously available. In this study, we present the structure of wild-type MexAB–OprM in the presence or absence of drugs at near-atomic resolution. The structure reveals that OprM does not interact with MexB directly, and that it opens its periplasmic gate by forming a complex. Furthermore, we confirm the residues essential for complex formation and observed a movement of the drug entrance gate. Based on these results, we propose mechanisms for complex formation and drug efflux

An extended star cluster at the outer edge of the spiral galaxy M33

We report a discovery of an extended globular-like star cluster, M33-EC1, at the outer edge of the spiral galaxy M33. The distance to the cluster is 890 kpc, and it lies at a 12.5 kpc projected distance from the center of M33. Old age (>~7 Gyr) and low metallicity ([M/H] <~ -1.4) are estimated on the basis of isochrone fits. Color-magnitude diagrams of stars, located in the cluster's area, photometric and structural parameters of the cluster are presented. Cluster's luminosity (M_V = -6.6) and half-light radius (r_h = 20.3 pc) are comparable to those of the extended globular clusters, discovered in more luminous Local Group galaxies, the Milky Way and M31. Extended globular clusters are suspected to be remnants of accreted dwarf galaxies, and the finding of such a cluster in the late-type dwarf spiral galaxy M33 would imply a complex merging history in the past.Comment: 20 pages, 6 figures, 2 tables, accepted for publication in A

Structure of a cyanobacterial photosystem I surrounded by octadecameric IsiA antenna proteins

Iron-stress induced protein A (IsiA) is a chlorophyll-binding membrane-spanning protein in photosynthetic prokaryote cyanobacteria, and is associated with photosystem I (PSI) trimer cores, but its structural and functional significance in light harvesting remains unclear. Here we report a 2.7-angstrom resolution cryo-electron microscopic structure of a supercomplex between PSI core trimer and IsiA from a thermophilic cyanobacterium Thermosynechococcus vulcanus. The structure showed that 18 IsiA subunits form a closed ring surrounding a PSI trimer core. Detailed arrangement of pigments within the supercomplex, as well as molecular interactions between PSI and IsiA and among IsiAs, were resolved. Time-resolved fluorescence spectra of the PSI-IsiA supercomplex showed clear excitation-energy transfer from IsiA to PSI, strongly indicating that IsiA functions as an energy donor, but not an energy quencher, in the supercomplex. These structural and spectroscopic findings provide important insights into the excitation-energy-transfer and subunit assembly mechanisms in the PSI-IsiA supercomplex. Akita et al. present the latest approach to solve IsiA-PSI supercomplex molecular structure with increased resolution using cryo-EM and time-resolved fluorescence studies. With 2.7 angstrom resolution, they reveal molecular interactions between PSI and IsiA subunits and that IsiA functions as an energy donor in the supercomplex

Structural basis for different types of hetero-tetrameric light-harvesting complexes in a diatom PSII-FCPII supercomplex

Fucoxanthin chlorophyll (Chl) a/c-binding proteins (FCPs) function as light harvesters in diatoms. The structure of a diatom photosystem II-FCPII (PSII-FCPII) supercomplex have been solved by cryo-electron microscopy (cryo-EM) previously; however, the FCPII subunits that constitute the FCPII tetramers and monomers are not identified individually due to their low resolutions. Here, we report a 2.5 angstrom resolution structure of the PSII-FCPII supercomplex using cryo-EM. Two types of tetrameric FCPs, S-tetramer, and M-tetramer, are identified as different types of hetero-tetrameric complexes. In addition, three FCP monomers, m1, m2, and m3, are assigned to different gene products of FCP. The present structure also identifies the positions of most Chls c and diadinoxanthins, which form a complicated pigment network. Excitation-energy transfer from FCPII to PSII is revealed by time-resolved fluorescence spectroscopy. These structural and spectroscopic findings provide insights into an assembly model of FCPII and its excitation-energy transfer and quenching processes. Fucoxanthin chlorophyll a/c-binding proteins (FCPs) harvest light energy in diatoms. The authors analyzed a structure of PSII-FCPII supercomplex at high resolution by cryo-EM, which identified each FCP subunit and pigment network in the supercomplex

Full-Fledged Dwarf Irregular Galaxy Leo A

We have studied Leo A - the isolated and extremely gas rich dwarf irregular galaxy of very low stellar mass and metallicity. Ages of the stellar populations in Leo A are ranging from ~10 Myr to ~10 Gyr. Here we report the discovery of an old stellar halo and a sharp stellar edge. Also we find the distribution of stars extending beyond the gaseous envelope of the galaxy. Therefore, Leo A by its structure as well as stellar and gaseous content is found to resemble massive disk galaxies. This implies that galaxies of very low stellar mass are also able to develop complex structures, challenging contemporary understanding of galaxy evolution.Comment: 9 pages, 3 figures, submitted to ApJ

Structural basis for the adaptation and function of chlorophyll f in photosystem I

Chlorophylls (Chl) play pivotal roles in energy capture, transfer and charge separation in photosynthesis. Among Chls functioning in oxygenic photosynthesis, Chl f is the most red-shifted type first found in a cyanobacterium Halomicronema hongdechloris. The location and function of Chl f in photosystems are not clear. Here we analyzed the high-resolution structures of photosystem I (PSI) core from H. hongdechloris grown under white or far-red light by cryo-electron microscopy. The structure showed that, far-red PSI binds 83 Chl a and 7 Chl f, and Chl f are associated at the periphery of PSI but not in the electron transfer chain. The appearance of Chl f is well correlated with the expression of PSI genes induced under far-red light. These results indicate that Chl f functions to harvest the far-red light and enhance uphill energy transfer, and changes in the gene sequences are essential for the binding of Chl f