HST/STIS Ultraviolet Imaging of Polar Aurora on Ganymede

We report new observations of the spectrum of Ganymede in the spectral range 1160 - 1720 A made with the Space Telescope Imaging Spectrograph (STIS) on HST on 1998 October 30. The observations were undertaken to locate the regions of the atomic oxygen emissions at 1304 and 1356 A, previously observed with the GHRS on HST, that Hall et al. (1998) claimed indicated the presence of polar aurorae on Ganymede. The use of the 2" wide STIS slit, slightly wider than the disk diameter of Ganymede, produced objective spectra with images of the two oxygen emissions clearly separated. The OI emissions appear in both hemispheres, at latitudes above 40 degrees, in accordance with recent Galileo magnetometer data that indicate the presence of an intrinsic magnetic field such that Jovian magnetic field lines are linked to the surface of Ganymede only at high latitudes. Both the brightness and relative north-south intensity of the emissions varied considerably over the four contiguous orbits (5.5 hours) of observation, presumably due to the changing Jovian plasma environment at Ganymede. However, the observed longitudinal non-uniformity in the emission brightness at high latitudes, particularly in the southern hemisphere, and the lack of pronounced limb brightening near the poles are difficult to understand with current models. In addition to observed solar HI Lyman-alpha reflected from the disk, extended Lyman-alpha emission resonantly scattered from a hydrogen exosphere is detected out to beyond two Ganymede radii from the limb, and its brightness is consistent with the Galileo UVS measurements of Barth et al. (1997).Comment: 7 pages, 4 figures, accepted for publication in ApJ, June 1, 200

Excitation of the Ganymede Ultraviolet Aurora

We analyze the ultraviolet aurorae observed on Ganymede by means of the Hubble Space Telescope and compare them to similar phenomena on Earth. We find that the tenuous nature of Ganymede's atmosphere precludes excitation of the aurora by high-energy electrons and requires a local acceleration mechanism. We propose the following as plausible mechanisms for generating both the continuous background emission and the intense auroral bright spots

Lyman‐α imaging of the SO 2 distribution on Io

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/94916/1/grl12620.pd

The Far Ultraviolet Spectral Signatures of Formaldehyde and Carbon Dioxide in Comets

Observations of four comets made with the Far Ultraviolet Spectroscopic Explorer show the rotational envelope of the (0,0) band of the CO Hopfield-Birge system (C - X) at 1088 A to consist of both "cold" and "hot" components, the "cold" component accounting for ~75% of the flux and with a rotational temperature in the range 55-75 K. We identify the "hot" component as coming from the dissociation of CO2 into rotationally "hot" CO, with electron impact dissociation probably dominant over photodissociation near the nucleus. An additional weak, broad satellite band is seen centered near the position of the P(40) line that we attribute to CO fluorescence from a non-thermal high J rotational population produced by photodissociation of formaldehyde into CO and H2. This process also leaves the H2 preferentially populated in excited vibrational levels which are identified by fluorescent H2 lines in the spectrum excited by solar OVI 1031.9 and solar Lyman-alpha. The amount of H2 produced by H2CO dissociation is comparable to the amount produced by photodissociation of H2O. Electron impact excitation of CO, rather than resonance fluorescence, appears to be the primary source of the observed (B - X) (0,0) band at 1151 A.Comment: 21 pages, 7 figures, accepted for publication in the Astrophysical Journa

ER-Bound Protein Tyrosine Phosphatase PTP1B Interacts with Src at the Plasma Membrane/Substrate Interface

PTP1B is an endoplasmic reticulum (ER) anchored enzyme whose access to substrates is partly dependent on the ER distribution and dynamics. One of these substrates, the protein tyrosine kinase Src, has been found in the cytosol, endosomes, and plasma membrane. Here we analyzed where PTP1B and Src physically interact in intact cells, by bimolecular fluorescence complementation (BiFC) in combination with temporal and high resolution microscopy. We also determined the structural basis of this interaction. We found that BiFC signal is displayed as puncta scattered throughout the ER network, a feature that was enhanced when the substrate trapping mutant PTP1B-D181A was used. Time-lapse and co-localization analyses revealed that BiFC puncta did not correspond to vesicular carriers; instead they localized at the tip of dynamic ER tubules. BiFC puncta were retained in ventral membrane preparations after cell unroofing and were also detected within the evanescent field of total internal reflection fluorescent microscopy (TIRFM) associated to the ventral membranes of whole cells. Furthermore, BiFC puncta often colocalized with dark spots seen by surface reflection interference contrast (SRIC). Removal of Src myristoylation and polybasic motifs abolished BiFC. In addition, PTP1B active site and negative regulatory tyrosine 529 on Src were primary determinants of BiFC occurrence, although the SH3 binding motif on PTP1B also played a role. Our results suggest that ER-bound PTP1B dynamically interacts with the negative regulatory site at the C-terminus of Src at random puncta in the plasma membrane/substrate interface, likely leading to Src activation and recruitment to adhesion complexes. We postulate that this functional ER/plasma membrane crosstalk could apply to a wide array of protein partners, opening an exciting field of research

Mutations at Residues 282, 286, and 293 of Phage λ Integrase Exert Pathway-Specific Effects on Synapsis and Catalysis in Recombination

Bacteriophage λ integrase (Int) catalyzes site-specific recombination between pairs of attachment (att) sites. The att sites contain weak Int-binding sites called core-type sites that are separated by a 7-bp overlap region, where cleavage and strand exchange occur. We have characterized a number of mutant Int proteins with substitutions at positions S282 (S282A, S282F, and S282T), S286 (S286A, S286L, and S286T), and R293 (R293E, R293K, and R293Q). We investigated the core- and arm-binding properties and cooperativity of the mutant proteins, their ability to catalyze cleavage, and their ability to form and resolve Holliday junctions. Our kinetic analyses have identified synapsis as the rate-limiting step in excisive recombination. The IntS282 and IntS286 mutants show defects in synapsis in the bent-L and excisive pathways, respectively, while the IntR293 mutants exhibit synapsis defects in both the excision and bent-L pathways. The results of our study support earlier findings that the catalytic domain also serves a role in binding to core-type sites, that the core contacts made by this domain are important for both synapsis and catalysis, and that Int contacts core-type sites differently among the four recombination pathways. We speculate that these residues are important for the proper positioning of the catalytic residues involved in the recombination reaction and that their positions differ in the distinct nucleoprotein architectures formed during each pathway. Finally, we found that not all catalytic events in excision follow synapsis: the attL site probably undergoes several rounds of cleavage and ligation before it synapses and exchanges DNA with attR