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lüll L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle Grallath S; Schwarz JP; Bottcher UM; Bracher A; Hartl FU; Siegers KEMBO Rep 2006[Jan]; 7 (1): 78-84The nascent chain-associated complex (NAC) is a dimeric protein complex of archaea and eukarya that interacts with ribosomes and translating polypeptide chains. We show that, in yeast, NAC and the signal-recognition particle (SRP) share the universally conserved ribosomal protein L25 as a docking site, which is in close proximity to the ribosomal exit tunnel. The amino-terminal segment of beta-NAC was found to be required for L25 binding. Purified NAC can prevent protein aggregation in vitro and thus shows certain properties of a molecular chaperone. Interestingly, the alpha-subunit of NAC interacts with the 54 kDa subunit of SRP. Consistent with a regulatory role of NAC in protein translocation into the endoplasmic reticulum (ER), we find that deletion of NAC results in an induction of the ER stress-response pathway. These results identify L25 as a conserved interaction platform for specific cytosolic factors that guide nascent polypeptides to their proper cellular destination.|Archaeal Proteins/genetics/metabolism[MESH]|Fungal Proteins/genetics/*metabolism[MESH]|Multiprotein Complexes[MESH]|Protein Biosynthesis[MESH]|Protein Structure, Tertiary[MESH]|Protein Subunits/genetics/metabolism[MESH]|Ribosomal Proteins/genetics/*metabolism[MESH]|Ribosomes/*metabolism[MESH]|Signal Recognition Particle/*metabolism[MESH]|Two-Hybrid System Techniques[MESH] |