Molecular architecture of the yeast Elongator complex reveals an unexpected asymmetric subunit arrangement.
作者： Dheva T Setiaputra , Derrick TH Cheng , Shan Lu , Jesse M Hansen , Udit Dalwadi
关键词:
摘要: Elongator is a ~850 kDa protein complex involved in multiple processes from transcription to tRNA modification. Conserved yeast humans, assembled two copies of six unique subunits (Elp1 Elp6). Despite the wealth structural data on individual subunits, overall architecture and subunit organization full molecular mechanisms how it exerts its activities remain unclear. Using single-particle electron microscopy (EM), we revealed that adopts bilobal an unexpected asymmetric arrangement resulting hexameric Elp456 subassembly anchored one Elp123 lobes form scaffold. By integrating EM with available crystal structures restraints generated cross-linking coupled mass spectrometry, constructed multiscale model showed Elp3, main catalytic subunit, are located distinct environments. This work provides first insights into framework understand basis multifunctionality.
sci-hub.se 参考文章(42)
Lawrence A Kelley, Stefans Mezulis, Christopher M Yates, Mark N Wass, Michael J E Sternberg, The Phyre2 web portal for protein modeling, prediction and analysis Nature Protocols. ,vol. 10, pp. 845- 858 ,(2015) , 10.1038/NPROT.2015.053
Chunming Dong, Zhijie Lin, Wentao Diao, Dan Li, Xinlei Chu, Zheng Wang, Hao Zhou, Zhiping Xie, Yuequan Shen, Jiafu Long, The Elp2 subunit is essential for elongator complex assembly and functional regulation Structure. ,vol. 23, pp. 1078- 1086 ,(2015) , 10.1016/J.STR.2015.03.018
Eric D. Merkley, Steven Rysavy, Abdullah Kahraman, Ryan P. Hafen, Valerie Daggett, Joshua N. Adkins, Distance restraints from crosslinking mass spectrometry: Mining a molecular dynamics simulation database to evaluate lysine–lysine distances Protein Science. ,vol. 23, pp. 747- 759 ,(2014) , 10.1002/PRO.2458
Qing Li, A. M. Fazly, Hui Zhou, Shengbing Huang, Zhiguo Zhang, Bruce Stillman, The elongator complex interacts with PCNA and modulates transcriptional silencing and sensitivity to DNA damage agents PLOS Genetics. ,vol. 5, ,(2009) , 10.1371/JOURNAL.PGEN.1000684
Nils A Kulak, Garwin Pichler, Igor Paron, Nagarjuna Nagaraj, Matthias Mann, None, Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells. Nature Methods. ,vol. 11, pp. 319- 324 ,(2014) , 10.1038/NMETH.2834
Berthold Kastner, Niels Fischer, Monika Mariola Golas, Bjoern Sander, Prakash Dube, Daniel Boehringer, Klaus Hartmuth, Jochen Deckert, Florian Hauer, Elmar Wolf, Hannes Uchtenhagen, Henning Urlaub, Franz Herzog, Jan Michael Peters, Dietmar Poerschke, Reinhard Lührmann, Holger Stark, GraFix: sample preparation for single-particle electron cryomicroscopy Nature Methods. ,vol. 5, pp. 53- 55 ,(2008) , 10.1038/NMETH1139
Sebastian Glatt, Christoph W Müller, Structural insights into Elongator function Current Opinion in Structural Biology. ,vol. 23, pp. 235- 242 ,(2013) , 10.1016/J.SBI.2013.02.009
David L. Tabb, W. Hayes McDonald, John R. Yates, DTASelect and Contrast: Tools for Assembling and Comparing Protein Identifications from Shotgun Proteomics Journal of Proteome Research. ,vol. 1, pp. 21- 26 ,(2002) , 10.1021/PR015504Q
Catherine Creppe, Lina Malinouskaya, Marie-Laure Volvert, Magali Gillard, Pierre Close, Olivier Malaise, Sophie Laguesse, Isabelle Cornez, Souad Rahmouni, Sandra Ormenese, Shibeshih Belachew, Brigitte Malgrange, Jean-Paul Chapelle, Ulrich Siebenlist, Gustave Moonen, Alain Chariot, Laurent Nguyen, None, Elongator Controls the Migration and Differentiation of Cortical Neurons through Acetylation of α-Tubulin Cell. ,vol. 136, pp. 551- 564 ,(2009) , 10.1016/J.CELL.2008.11.043
Gabriel Otero, Jane Fellows, Yang Li, Therese de Bizemont, Annette M.G Dirac, Claes M Gustafsson, Hediye Erdjument-Bromage, Paul Tempst, Jesper Q Svejstrup, Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. Molecular Cell. ,vol. 3, pp. 109- 118 ,(1999) , 10.1016/S1097-2765(00)80179-3