Building arks for tRNA: structure and function of the Arc1p family of non-catalytic tRNA-binding proteins.
Following 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 prokaryotes and higher eukaryotes. They represent paradigms of the strategies employed for the organization of sophisticated and dynamic nanostructures supporting spatio-temporal cellular organization.
Karanasios
Eleftherios
E
Laboratory of Biochemistry, School of Medicine, University of Thessaly, BIOPOLIS, Larissa, Greece. ek340@cam.ac.uk
Simos
George
G
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D016207:Cytokines / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D009363:Neoplasm Proteins / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D012343:RNA, Transfer / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D046249:Transfer RNA Aminoacylation; D000099253:Trans-Activation Responsive RNA-Binding Protein
D001426:Bacterial Proteins; D016207:Cytokines; D009363:Neoplasm Proteins; D012343:RNA, Transfer; D016601:RNA-Binding Proteins; D029701:Saccharomyces cerevisiae Proteins; D000099253:Trans-Activation Responsive RNA-Binding Protein; C102145:ARC1 protein, S cerevisiae; C120618:Trbp111 protein, Aquifex aeolicus; C077219:small inducible cytokine subfamily E, member 1