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dc.creatorKaranasios, E.en
dc.creatorSimos, G.en
dc.date.accessioned2015-11-23T10:33:16Z
dc.date.available2015-11-23T10:33:16Z
dc.date.issued2010
dc.identifier10.1016/j.febslet.2010.08.023
dc.identifier.issn0014-5793
dc.identifier.urihttp://hdl.handle.net/11615/29029
dc.description.abstractFollowing the intricate architecture of the eukaryotic cell, protein synthesis involves formation of many macromolecular assemblies, some of which are composed by tRNA-aminoacylation enzymes. Protein-protein and protein-tRNA interactions in these complexes can be facilitated by non-catalytic tRNA-binding proteins. This review focuses on the dissection of the molecular, structural and functional properties of a particular family of such proteins: yeast Arc1p and its homologues in pro-karyotes and higher eukaryotes. They represent paradigms of the strategies employed for the organization of sophisticated and dynamic nanostructures supporting spatio-temporal cellular organization. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.en
dc.sourceFebs Lettersen
dc.source.uri<Go to ISI>://WOS:000282187500003
dc.subjecttRNAen
dc.subjectArc1pen
dc.subjectTrbp111en
dc.subjectp43en
dc.subjectp38en
dc.subjectp18en
dc.subjectMETHIONYL-TRANSFER-RNAen
dc.subjectAMINOACYLATION COFACTOR ARC1Pen
dc.subjectACTIVATINGen
dc.subjectPOLYPEPTIDE-IIen
dc.subjectSYNTHETASE COMPLEXen
dc.subjectSACCHAROMYCES-CEREVISIAEen
dc.subjectMULTISYNTHETASE COMPLEXen
dc.subjectP43 COMPONENTen
dc.subjectMACROMOLECULAR ASSEMBLAGEen
dc.subjectTERMINAL EXTENSIONen
dc.subjectCRYSTAL-STRUCTUREen
dc.subjectBiochemistry & Molecular Biologyen
dc.subjectBiophysicsen
dc.subjectCell Biologyen
dc.titleBuilding arks for tRNA: Structure and function of the Arc1p family of non-catalytic tRNA-binding proteinsen
dc.typejournalArticleen


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