Dataset Information

S.lividans TK24 protease deletions

ABSTRACT: Characterization of S.lividans TK24 secreted proteome changes upon deletion of certain proteases.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Streptomyces Lividans Tk24

SUBMITTER: Konstantinos Tsolis

LAB HEAD: Tassos Economou

PROVIDER: PXD006819 | Pride | 2018-06-28

REPOSITORIES: Pride

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Publications

Multi-Omics and Targeted Approaches to Determine the Role of Cellular Proteases in Streptomyces Protein Secretion.

Busche Tobias T Tsolis Konstantinos C KC Koepff Joachim J Rebets Yuriy Y Rückert Christian C Hamed Mohamed B MB Bleidt Arne A Wiechert Wolfgang W Lopatniuk Mariia M Yousra Ahmed A Anné Jozef J Karamanou Spyridoula S Oldiges Marco M Kalinowski Jörn J Luzhetskyy Andriy A Economou Anastassios A

Frontiers in microbiology 20180604

Gram-positive Streptomyces bacteria are profuse secretors of polypeptides using complex, yet unknown mechanisms. Many of their secretory proteins are proteases that play important roles in the acquisition of amino acids from the environment. Other proteases regulate cellular proteostasis. To begin dissecting the possible role of proteases in Streptomyces secretion, we applied a multi-omics approach. We probed the role of the 190 proteases of Streptomyces lividans strain TK24 ...[more]

PMID: 29915569

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Project description:Proline-rich antimicrobial peptide apidaecin (Api) inhibits bacterial protein synthesis in a distinctive way. In vitro biochemical and structural studies showed that Api binds in the nascent peptide exit tunnel of the ribosome that has completed translation of the gene and has released the newly-synthesized protein. Once in the tunnel, Api traps the release factors on the post-termination ribosome leading to cessation of translation. The mode of Api action in the bacterial cell, however, had remained unknow. By analyzing distribution of ribosomes on mRNAs in Api-treated cells using Ribo-seq approach we uncovered a range of effects that stem from the unique mechanism of Api action. Exposure of bacterial cells to Api results in arrest of translation at stop codons, likely in a post-release state, due to the immediate Api action, as well as in a pre-release state due to the depletion of available release factors. In addition, arrest of translation at the end of the open reading frame (ORF) leads to a pronounced queuing of the translating ribosomes behind the one arrested at the stop codon. One of the major consequences of the Api action is a dramatically increased stop codon bypass by the ribosomes paused in a pre-release state, leading to accumulation of proteins with C-terminal extensions, as confirmed by whole-cell proteomics analysis. Stop codon bypass, that occurs either in 0-frame, by misincorporation of a near-cognate aminoacyl-tRNA at the stop codon, or via frameshifting allows for a fraction of the translating ribosomes to reach the 3’ ends of mRNA transcripts. The pervasive stalling of pre-release ribosomes at the stop codons and at the RNA transcripts ends triggers activation of the cellular ribosome rescue systems which, likely due to Api action as well, remain ineffective. While major Api effects are directed towards the ribosome at the end of the ORFs, cells exposed to Api show a somewhat increased ribosome occupancy of the start codons. Understanding the unique mode of Api to inhibit translation termination in the cell can help envisioning the development of treatments for genetic diseases and research tools for genome exploration.

Dataset Information

S.lividans TK24 protease deletions

Publications

Multi-Omics and Targeted Approaches to Determine the Role of Cellular Proteases in <i>Streptomyces</i> Protein Secretion.

Similar Datasets

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