Multitasking SecB chaperones in bacteria

Sala, Ambre; Bordes, Patricia; Genevaux, Pierre

doi:10.3389/fmicb.2014.00666

Cited by 71 publications

(56 citation statements)

References 129 publications

(178 reference statements)

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“…5). These new TAC systems are thus representatives of the three different antitoxin families found associated with a SecB-like chaperone in bacterial genomes1011.…”

Section: Resultsmentioning

confidence: 99%

“…Grafting chaperone/ChAD modules to specific protein targets might thus represent a valuable tool to optimize the expression and folding of difficult heterologous proteins expressed in E. coli for biotechnological or medical purposes. Since a significant number of SecB sequences (over 7%) are associated with TA systems, it is very likely that this represents an important reservoir of unexplored specific chaperone/ChAD cognates11.…”

Section: Discussionmentioning

confidence: 99%

“…Tripartite toxin–antitoxin–chaperone (TAC) systems are atypical TA modules composed of a two-component type II TA, generally belonging to the well-conserved HigBA, HicAB or MqsRA TA families, and a molecular chaperone homologous to the export chaperone SecB, located on the same operon1011. To date, the TAC system of the major human pathogen Mycobacterium tuberculosis is the best characterized41012.…”

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confidence: 99%

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Chaperone addiction of toxin–antitoxin systems

et al. 2016

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Bacterial toxin–antitoxin (TA) systems, in which a labile antitoxin binds and inhibits the toxin, can promote adaptation and persistence by modulating bacterial growth in response to stress. Some atypical TA systems, known as tripartite toxin–antitoxin–chaperone (TAC) modules, include a molecular chaperone that facilitates folding and protects the antitoxin from degradation. Here we use a TAC module from Mycobacterium tuberculosis as a model to investigate the molecular mechanisms by which classical TAs can become ‘chaperone-addicted'. The chaperone specifically binds the antitoxin at a short carboxy-terminal sequence (chaperone addiction sequence, ChAD) that is not present in chaperone-independent antitoxins. In the absence of chaperone, the ChAD sequence destabilizes the antitoxin, thus preventing toxin inhibition. Chaperone–ChAD pairs can be transferred to classical TA systems or to unrelated proteins and render them chaperone-dependent. This mechanism might be used to optimize the expression and folding of heterologous proteins in bacterial hosts for biotechnological or medical purposes.

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“…5). These new TAC systems are thus representatives of the three different antitoxin families found associated with a SecB-like chaperone in bacterial genomes1011.…”

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Chaperone addiction of toxin–antitoxin systems

et al. 2016

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“…The common systems in bacteria are the Sec, YidC and TAT translocons. The Sec (secretory) system threads translated polypeptide chains in an unfolded form to the periplasm, which is associated with the cleavage of an N-terminal leader sequence by a specific peptidase (du Plessis, Nouwen, & Driessen, 2011;Paetzel, 2014;Sala, Bordes, & Genevaux, 2014). The Sec system is assisted by the YidC protein, which correctly inserts TMHs (Dalbey, Kuhn, Zhu, & Kiefer, 2014).…”

Section: Assembly Of Bacterial Respiratory Complexesmentioning

confidence: 99%

Bacterial Electron Transfer Chains Primed by Proteomics

Wessels¹,

Almeida²,

Kartal³

et al. 2016

Advances in Bacterial Electron Transport Systems and Their Regulation

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Electron transport phosphorylation is the central mechanism for most prokaryotic species to harvest energy released in the respiration of their substrates as ATP. Microorganisms have evolved incredible variations on this principle, most of these we perhaps do not know, considering that only a fraction of the microbial richness is known. Besides these variations, microbial species may show substantial versatility in using respiratory systems. In connection herewith, regulatory mechanisms control the expression of these respiratory enzyme systems and their assembly at the translational and posttranslational levels, to optimally accommodate changes in the supply of their energy substrates. Here, we present an overview of methods and techniques from the field of proteomics to explore bacterial electron transfer chains and their regulation at levels ranging from the whole organism down to the Ångstrom scales of protein structures. From the survey of the literature on this subject, it is concluded that proteomics, indeed, has substantially contributed to our comprehending of bacterial respiratory mechanisms, often in elegant combinations with genetic and biochemical approaches. However, we also note that advanced proteomics offers a wealth of opportunities, which have not been exploited at all, or at best underexploited in hypothesis-driving and hypothesis-driven research on bacterial bioenergetics. Examples obtained from the related area of mitochondrial oxidative phosphorylation research, where the application of advanced proteomics is more common, may illustrate these opportunities.

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“…In bacteria, another translocation pathway, which recruits nascent outer membrane proteins and periplasmic proteins, involves the ATPase motor protein SecA and the chaperone SecB [114][115][116]. In chloroplasts, only SecA is found.…”

Section: Co-translational Targeting Of Chloroplast-encoded Proteins Tmentioning

confidence: 99%

Co-Translational Protein Folding and Sorting in Chloroplasts

Ries

Herkt

Willmund

2020

Plants

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Cells depend on the continuous renewal of their proteome composition during the cell cycle and in order to replace aberrant proteins or to react to changing environmental conditions. In higher eukaryotes, protein synthesis is achieved by up to five million ribosomes per cell. With the fast kinetics of translation, the large number of newly made proteins generates a substantial burden for protein homeostasis and requires a highly orchestrated cascade of factors promoting folding, sorting and final maturation. Several of the involved factors directly bind to translating ribosomes for the early processing of emerging nascent polypeptides and the translocation of ribosome nascent chain complexes to target membranes. In plant cells, protein synthesis also occurs in chloroplasts serving the expression of a relatively small set of 60–100 protein-coding genes. However, most of these proteins, together with nucleus-derived subunits, form central complexes majorly involved in the essential processes of photosynthetic light reaction, carbon fixation, metabolism and gene expression. Biogenesis of these heterogenic complexes adds an additional level of complexity for protein biogenesis. In this review, we summarize the current knowledge about co-translationally binding factors in chloroplasts and discuss their role in protein folding and ribosome translocation to thylakoid membranes.

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Multitasking SecB chaperones in bacteria

Cited by 71 publications

References 129 publications

Chaperone addiction of toxin–antitoxin systems

Chaperone addiction of toxin–antitoxin systems

Bacterial Electron Transfer Chains Primed by Proteomics

Co-Translational Protein Folding and Sorting in Chloroplasts

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