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Rainer Schimmel,Dariusz Tarnawski 한국응용곤충학회 2016 Journal of Asia-Pacific Entomology Vol.19 No.3
Three new species of Costalicus gen. nov. are described from northern Pakistan: C. kaghanensis sp. nov., C. pakistanus sp. nov. and C. sulcatus sp. nov. The new genus is morphologically very similar to the genus Mosotalesus Kishii, 1977 but differs distinctly in the costiform structure of the elytral striae intervals, the conspicuously broad and crown-shaped elytral lateral edge, long and distinctly arched carina, and in the obtuse apices of pronotal basal angles. All specimens of the new species were collected in the western Himalaya at 3000–4000 m a.s.l. The new genus belongs to the tribe Prosternini Gistel, 1856.
Rainer Schimmel,Dariusz Tarnawski 한국응용곤충학회 2017 Journal of Asia-Pacific Entomology Vol.20 No.1
Two newspecies fromthe genera Calambus Thomson 1859 and Hypoganus Kiesenwetter, 1858 (tribe Prosternini Gistel, 1856), fromChina are described and illustrated. These are the first species of Calambus and the second species of Hypoganus recorded from China. Additionally, we provide distributional data for Hypoganus tibetis Čechovský and Kubáň 1997.
Trp-tRNA synthetase bridges DNA-PKcs to PARP-1 to link IFN-款 and p53 signaling
Sajish, Mathew,Zhou, Quansheng,Kishi, Shuji,Valdez Jr, Delgado M,Kapoor, Mili,Guo, Min,Lee, Sunhee,Kim, Sunghoon,Yang, Xiang-Lei,Schimmel, Paul Nature Publishing Group, a division of Macmillan P 2012 NATURE CHEMICAL BIOLOGY Vol.8 No.6
Interferon-款 (IFN-款) engenders strong antiproliferative responses, in part through activation of p53. However, the long-known IFN-款??dependent upregulation of human Trp-tRNA synthetase (TrpRS), a cytoplasmic enzyme that activates tryptophan to form Trp-AMP in the first step of protein synthesis, is unexplained. Here we report a nuclear complex of TrpRS with the catalytic subunit of DNA-dependent protein kinase (DNA-PKcs) and with poly(ADP-ribose) polymerase 1 (PARP-1), the major PARP in human cells. The IFN-款??dependent poly(ADP-ribosyl)ation of DNA-PKcs (which activates its kinase function) and concomitant activation of the tumor suppressor p53 were specifically prevented by Trp-SA, an analog of Trp-AMP that disrupted the TrpRS??DNA-PKcs??PARP-1 complex. The connection of TrpRS to p53 signaling in vivo was confirmed in a vertebrate system. These and further results suggest an unexpected evolutionary expansion of the protein synthesis apparatus to a nuclear role that links major signaling pathways.
Secreted human glycyl-tRNA synthetase implicated in defense against ERK-activated tumorigenesis
Park, M. C.,Kang, T.,Jin, D.,Han, J. M.,Kim, S. B.,Park, Y. J.,Cho, K.,Park, Y. W.,Guo, M.,He, W.,Yang, X.-L.,Schimmel, P.,Kim, S. Proceedings of the National Academy of Sciences 2012 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.109 No.11
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.