670 research outputs found
An Infrared Study of the Large-scale Jet in Quasar PKS 1136-135
We present Spitzer IRAC imaging of the large-scale jet in the quasar PKS
1136-135 at wavelengths of 3.6 and 5.8 um, combined with previous VLA, HST, and
Chandra observations. We clearly detect infrared emission from the jet,
resulting in the most detailed multifrequency data among the jets in
lobe-dominated quasars. The spectral energy distributions of the jet knots have
significant variations along the jet, like the archetypal jet in 3C 273. The
infrared measurements with IRAC are consistent with the previous idea that the
jet has two spectral components, namely (1) the low-energy synchrotron spectrum
extending from radio to infrared, and (2) the high-energy component responsible
for the X-ray flux. The optical fluxes may be a mixture of the two components.
We consider three radiation models for the high-energy component: inverse
Compton scattering off CMB photons by radio-emitting electrons in a highly
relativistic jet, synchrotron radiation by a second distinct electron
population, and synchrotron radiation by ultra high energy protons. Each
hypothesis leads to important insights into and constraints on particle
acceleration in the jet, as well as the basic physical properties of the jet
such as bulk velocity, transporting power, and particle contents.Comment: 9 pages, 5 figures (2 color figures), accepted for publication in
ApJ; one typo in Table 1 is correcte
Radio Continuum Emission at 1.4 GHz from KISS Emission-Line Galaxies
We have searched the Faint Images of the Radio Sky at Twenty centimeters
(FIRST) and the NRAO VLA Sky Survey (NVSS) 1.4 GHz radio surveys for sources
that are coincident with emission-line galaxy (ELG) candidates from the KPNO
International Spectroscopic Survey (KISS). A total of 207 of the 2157 KISS ELGs
(~10%) in the first two H-alpha-selected survey lists were found to possess
radio detections in FIRST and/or NVSS. Follow-up spectra exist for all of the
radio detections, allowing us to determine the activity type (star-forming vs.
AGN) for the entire sample. We explore the properties of the radio-detected
KISS galaxies in order to gain a better insight into the nature of
radio-emitting galaxies in the local universe (z < 0.1). No dwarf galaxies were
detected, despite the large numbers of low-luminosity galaxies present in KISS,
suggesting that lower mass, lower luminosity objects do not possess strong
galaxian-scale magnetic fields. Due to the selection technique used for KISS,
our radio ELGs represent a quasi-volume-limited sample, which allows us to
develop a clearer picture of the radio galaxy population at low redshift.
Nearly 2/3rds of the KISS radio galaxies are starburst/star-forming galaxies,
which is in stark contrast to the results of flux-limited radio surveys that
are dominated by AGNs and elliptical galaxies (i.e., classic radio galaxies).
While there are many AGNs among the KISS radio galaxies, there are no objects
with large radio powers in our local volume. We derive a radio luminosity
function (RLF) for the KISS ELGs that agrees very well with previous RLFs that
adequately sample the lower-luminosity radio population.Comment: Accepted for publication in the Astronomical Journal (April 2004); 23
pages, 16 figure
SMA-Causing Missense Mutations in \u3cem\u3eSurvival motor neuron (Smn)\u3c/em\u3e Display a Wide Range of Phenotypes When Modeled in \u3cem\u3eDrosophila\u3c/em\u3e
Mutations in the human survival motor neuron 1 (SMN) gene are the primary cause of spinal muscular atrophy (SMA), a devastating neuromuscular disorder. SMN protein has a well-characterized role in the biogenesis of small nuclear ribonucleoproteins (snRNPs), core components of the spliceosome. Additional tissue-specific and global functions have been ascribed to SMN; however, their relevance to SMA pathology is poorly understood and controversial. Using Drosophila as a model system, we created an allelic series of twelve Smn missense mutations, originally identified in human SMA patients. We show that animals expressing these SMA-causing mutations display a broad range of phenotypic severities, similar to the human disease. Furthermore, specific interactions with other proteins known to be important for SMN\u27s role in RNP assembly are conserved. Intragenic complementation analyses revealed that the three most severe mutations, all of which map to the YG box self-oligomerization domain of SMN, display a stronger phenotype than the null allele and behave in a dominant fashion. In support of this finding, the severe YG box mutants are defective in self-interaction assays, yet maintain their ability to heterodimerize with wild-type SMN. When expressed at high levels, wild-type SMN is able to suppress the activity of the mutant protein. These results suggest that certain SMN mutants can sequester the wild-type protein into inactive complexes. Molecular modeling of the SMN YG box dimer provides a structural basis for this dominant phenotype. These data demonstrate that important structural and functional features of the SMN YG box are conserved between vertebrates and invertebrates, emphasizing the importance of self-interaction to the proper functioning of SMN. Author Summary
Spinal Muscular Atrophy (SMA) is a prevalent childhood neuromuscular disease, which in its most common form causes death by the age of two. One in fifty Americans is a carrier for SMA, making this genetic disease a serious health concern. SMA is caused by loss of function mutations in the survival motor neuron 1 (SMN1) gene. SMN is an essential protein and has a well-characterized function in the assembly of small nuclear ribonucleoproteins (snRNPs), which are core components of the spliceosome. To elucidate the phenotypic consequences of disrupting specific SMN protein interactions, we have generated a series of SMA-causing point mutations, modeled in Drosophila melanogaster. Using this system, we have shown that key aspects of SMN structure and function are conserved between humans and flies. Intragenic complementation analyses reveal the potential for dominant negative interactions between wild-type and mutant SMN subunits, highlighting the essential nature of the YG box in formation of higher-order SMN multimers. These results provide a basis for future studies investigating therapy targeted at restoration of functional SMN oligomers
Between the hammer and the anvil? The anti-money laundering-complex and its interactions with the compliance industry
International audienc
Shedding New Light on the 3C 273 Jet with the Spitzer Space Telescope
We have performed infrared imaging of the jet of the quasar 3C 273 at
wavelengths 3.6 and 5.8 microns with the Infrared Array Camera (IRAC) on the
Spitzer Space Telescope. When combined with the radio, optical and X-ray
measurements, the IRAC photometry clearly shows that the optical emission is
dominated by the high-energy component of the jet, not by the radio synchrotron
component, as had been assumed to date. The high-energy component may be due to
a second synchrotron component or to IC scattering of ambient photons. In the
former case, we argue that the acceleration of protons exceeding 10^16 eV or
possibly even to 10^19 eV would be taking place in the jet. In contrast, the IC
model, into which highly relativistic Doppler beaming has to be incorporated,
requires very low-energy electrons (~ 1 MeV). The present polarization data in
the radio and optical would favor the former interpretation in the case of the
3C 273 jet. Sensitive and detailed measurements of optical polarization are
important to establish the radiation mechanism responsible for the high-energy
emission. The present study offers new clues as to the controversial origin of
the X-ray emission seen in many quasar jets.Comment: 12 pages, 8 figures (2 color figures), accepted for publication in
ApJ, color images are also available at
http://www.astro.isas.jaxa.jp/~uchiyama/Site2/Spitzer_3C273.htm
Chromosomes. CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere
Inheritance of each chromosome depends upon its centromere. A histone H3 variant, centromere protein A (CENP-A), is essential for epigenetically marking centromere location. We find that CENP-A is quantitatively retained at the centromere upon which it is initially assembled. CENP-C binds to CENP-A nucleosomes and is a prime candidate to stabilize centromeric chromatin. Using purified components, we find that CENP-C reshapes the octameric histone core of CENP-A nucleosomes, rigidifies both surface and internal nucleosome structure, and modulates terminal DNA to match the loose wrap that is found on native CENP-A nucleosomes at functional human centromeres. Thus, CENP-C affects nucleosome shape and dynamics in a manner analogous to allosteric regulation of enzymes. CENP-C depletion leads to rapid removal of CENP-A from centromeres, indicating their collaboration in maintaining centromere identity.NIH grants: (GM082989, CA186430, GM008275, GM008216, GM007229); American Heart Association predoctoral fellowship; American Cancer Society postdoctoral fellowship; NSF grant: (agreement DMR-0944772)
Recommended from our members
Core-Shell Gold Nanorod@Zirconium-Based Metal-Organic Framework Composites as in Situ Size-Selective Raman Probes.
Nanoparticle encapsulation inside zirconium-based metal-organic frameworks (NP@MOF) is hard to control, and the resulting materials often have nonuniform morphologies with NPs on the external surface of MOFs and NP aggregates inside the MOFs. In this work, we report the controlled encapsulation of gold nanorods (AuNRs) by a scu-topology Zr-MOF, via a room-temperature MOF assembly. This is achieved by functionalizing the AuNRs with poly(ethylene glycol) surface ligands, allowing them to retain colloidal stability in the precursor solution and to seed the MOF growth. Using this approach, we achieve core-shell yields exceeding 99%, tuning the MOF particle size via the solution concentration of AuNRs. The functionality of AuNR@MOFs is demonstrated by using the AuNRs as embedded probes for selective surface-enhanced Raman spectroscopy (SERS). The AuNR@MOFs are able to both take-up or block molecules from the pores, thereby facilitating highly selective sensing at the AuNR ends. This proof-of-principle study serves to present both the outstanding level of control in the synthesis and the high potential for AuNR@Zr-MOF composites for SERS
The C-Terminal Domain of the Arabinosyltransferase Mycobacterium tuberculosis EmbC Is a Lectin-Like Carbohydrate Binding Module
The D-arabinan-containing polymers arabinogalactan (AG) and lipoarabinomannan (LAM) are essential components of the unique cell envelope of the pathogen Mycobacterium tuberculosis. Biosynthesis of AG and LAM involves a series of membrane-embedded arabinofuranosyl (Araf) transferases whose structures are largely uncharacterised, despite the fact that several of them are pharmacological targets of ethambutol, a frontline drug in tuberculosis therapy. Herein, we present the crystal structure of the C-terminal hydrophilic domain of the ethambutol-sensitive Araf transferase M. tuberculosis EmbC, which is essential for LAM synthesis. The structure of the C-terminal domain of EmbC (EmbCCT) encompasses two sub-domains of different folds, of which subdomain II shows distinct similarity to lectin-like carbohydrate-binding modules (CBM). Co-crystallisation with a cell wall-derived di-arabinoside acceptor analogue and structural comparison with ligand-bound CBMs suggest that EmbCCT contains two separate carbohydrate binding sites, associated with subdomains I and II, respectively. Single-residue substitution of conserved tryptophan residues (Trp868, Trp985) at these respective sites inhibited EmbC-catalysed extension of LAM. The same substitutions differentially abrogated binding of di- and penta-arabinofuranoside acceptor analogues to EmbCCT, linking the loss of activity to compromised acceptor substrate binding, indicating the presence of two separate carbohydrate binding sites, and demonstrating that subdomain II indeed functions as a carbohydrate-binding module. This work provides the first step towards unravelling the structure and function of a GT-C-type glycosyltransferase that is essential in M. tuberculosis. Author Summary Top Tuberculosis (TB), an infectious disease caused by the bacillus Mycobacterium tuberculosis, burdens large swaths of the world population. Treatment of active TB typically requires administration of an antibiotic cocktail over several months that includes the drug ethambutol. This front line compound inhibits a set of arabinosyltransferase enzymes, called EmbA, EmbB and EmbC, which are critical for the synthesis of arabinan, a vital polysaccharide in the pathogen's unique cell envelope. How precisely ethambutol inhibits arabinosyltransferase activity is not clear, in part because structural information of its pharmacological targets has been elusive. Here, we report the high-resolution structure of the C-terminal domain of the ethambutol-target EmbC, a 390-amino acid fragment responsible for acceptor substrate recognition. Combining the X-ray crystallographic analysis with structural comparisons, site-directed mutagenesis, activity and ligand binding assays, we identified two regions in the C-terminal domain of EmbC that are capable of binding acceptor substrate mimics and are critical for activity of the full-length enzyme. Our results begin to define structure-function relationships in a family of structurally uncharacterised membrane-embedded glycosyltransferases, which are an important target for tuberculosis therapy
- …