PMID:15840820

Citation	Guillier, M, Allemand, F, Graffe, M, Raibaud, S, Dardel, F, Springer, M and Chiaruttini, C (2005) The N-terminal extension of Escherichia coli ribosomal protein L20 is important for ribosome assembly, but dispensable for translational feedback control. RNA 11:728-38
Abstract	The Escherichia coli autoregulatory ribosomal protein L20 consists of two structurally distinct domains. The C-terminal domain is globular and sits on the surface of the large ribosomal subunit whereas the N-terminal domain has an extended shape and penetrates deep into the RNA-rich core of the subunit. Many other ribosomal proteins have analogous internal or terminal extensions. However, the biological functions of these extended domains remain obscure. Here we show that the N-terminal tail of L20 is important for ribosome assembly in vivo. Indeed, a truncated version of L20 without its N-terminal tail is unable to complement the deletion of rplT, the gene encoding L20. In addition, this L20 truncation confers a lethal-dominant phenotype, suggesting that the N-terminal domain is essential for cell growth because it could be required for ribosome assembly. Supporting this hypothesis, partial deletions of the N-terminal tail of the protein are shown to cause a slow-growth phenotype due to altered ribosome assembly in vivo as large amounts of intermediate 40S ribosomal particles accumulate. In addition to being a ribosomal protein, L20 also acts as an autogenous repressor. Using L20 truncations, we also show that the N-terminal tail of L20 is dispensable for autogenous control.
Links	PubMed PMC1370758 Online version:10.1261/rna.7134305
Keywords	Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Molecular Weight; Nucleic Acid Conformation; Phenotype; Polyribosomes/chemistry; Polyribosomes/metabolism; Protein Biosynthesis; Protein Structure, Tertiary; RNA, Ribosomal, 23S/chemistry; RNA, Ribosomal, 23S/genetics; RNA, Ribosomal, 23S/metabolism; Ribosomal Proteins/chemistry; Ribosomal Proteins/genetics; Ribosomal Proteins/metabolism; Ribosomes/chemistry; Ribosomes/metabolism; Sequence Deletion/genetics
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