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Ishioka, R.,Wang, S.-Y.,Zhang, Z.-W.,Lehner, M. J.,Alcock, C.,Axelrod, T.,Bianco, F. B.,Byun, Y.-I.,Chen, W. P.,Cook, K. H.,Kim, D.-W.,King, S.-K.,Lee, T.,Marshall, S. L.,Protopapas, P.,Rice, J. A.,Sc American Institute of Physics 2014 The Astronomical journal Vol.147 No.4
<P>The Taiwanese-American Occultation Survey project is designed for the detection of stellar occultations by small-size Kuiper Belt Objects, and it has monitored selected fields along the ecliptic plane by using four telescopes with a 3 deg<SUP>2</SUP> field of view on the sky since 2005. We have analyzed data accumulated during 2005-2012 to detect variable stars. Sixteen fields with observations of more than 100 epochs were examined. We recovered 85 variables among a total of 158 known variable stars in these 16 fields. Most of the unrecovered variables are located in the fields observed less frequently. We also detected 58 variable stars which are not listed in the International Variable Star Index of the American Association of Variable Star Observers. These variable stars are classified as 3 RR Lyrae, 4 Cepheid, 1 δ Scuti, 5 Mira, 15 semi-regular, and 27 eclipsing binaries based on the periodicity and the profile of the light curves.</P>
Structural Switch of Lysyl-tRNA Synthetase between Translation and Transcription
Ofir-Birin, Y.,Fang, P.,Bennett, Steven P.,Zhang, H.M.,Wang, J.,Rachmin, I.,Shapiro, R.,Song, J.,Dagan, A.,Pozo, J.,Kim, S.,Marshall, Alan G.,Schimmel, P.,Yang, X.L.,Nechushtan, H.,Razin, E.,Guo, M. Cell Press 2013 Molecular Cell Vol.49 No.1
Lysyl-tRNA synthetase (LysRS), a component of the translation apparatus, is released from the cytoplasmic multi-tRNA synthetase complex (MSC) to activate the transcription factor MITF in stimulated mast cells through undefined mechanisms. Here we show that Ser207 phosphorylation provokes a new conformer of LysRS that inactivates its translational function but activates its transcriptional function. The crystal structure of an MSC subcomplex established that LysRS is held in the MSC by binding to the N terminus of the scaffold protein p38/AIMP2. Phosphorylation-created steric clashes at the LysRS domain interface disrupt its binding grooves for p38/AIMP2, releasing LysRS and provoking its nuclear translocation. This alteration also exposes the C-terminal domain of LysRS to bind to MITF and triggers LysRS-directed production of the second messenger Ap<SUB>4</SUB>A that activates MITF. Thus our results establish that a single conformational change triggered by phosphorylation leads to multiple effects driving an exclusive switch of LysRS function from translation to transcription.