Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.

Ribosomal proteins (r-proteins) are abundant, highly conserved, and multifaceted cellular proteins in all domains of life. Most r-proteins have RNA-binding properties and can form protein-protein contacts. Bacterial r-proteins govern the co-transcriptional rRNA folding during ribosome assembly and participate in the formation of the ribosome functional sites, such as the mRNA-binding site, tRNA-binding sites, the peptidyl transferase center, and the protein exit tunnel.

Dynamic Transcriptional Landscape of under Cold Stress.

Bacterial adaptation to cold stress requires wide transcriptional reprogramming. However, the knowledge of molecular mechanisms underlying the cold stress response of mycobacteria is limited. We conducted comparative transcriptomic analysis of subjected to cold shock.

Regulation of Ribosomal Protein Synthesis in Mycobacteria: The Autogenous Control of .

The autogenous regulation of ribosomal protein (r-protein) synthesis plays a key role in maintaining the stoichiometry of ribosomal components in bacteria. In this work, taking the gene as a classic example, we addressed for the first time the in vivo regulation of r-protein synthesis in the mycobacteria () and (). We used a strategy based on chromosomally integrated reporters under the control of the regulatory regions and the ectopic expression of S15 to measure its impact on the reporter expression.

Autogenous regulation in vivo of the gene encoding ribosomal protein L31 (bL31), a key component of the protein-protein intersubunit bridge B1b.

Bacterial ribosomal proteins (r-proteins) encoded by nonessential genes often carry out very important tasks in translation. In particular, this is the case of a small basic bacteria-specific r-protein L31 (bL31). Recent studies revealed a crucial role of bL31 in formation of the protein-protein intersubunit bridge B1b and hence its contribution to ribosome dynamics.

Regulation of Ribosomal Protein Operons rplM-rpsI, rpmB-rpmG, and rplU-rpmA at the Transcriptional and Translational Levels.

Unlabelled: It is widely assumed that in the best-characterized model bacterium Escherichia coli, transcription units encoding ribosomal proteins (r-proteins) and regulation of their expression have been already well defined. However, transcription start sites for several E. coli r-protein operons have been established only very recently, so that information concerning the regulation of these operons at the transcriptional or posttranscriptional level is still missing.