YqjD Is an Inner Membrane Protein Associated with Stationary-Phase Ribosomes in Escherichia coli

Yoshida, Hideji; Maki, Yoshitaka; Furuike, Shou; Sakai, Akiko; Ueta, Masami; Wada, Akira

doi:10.1128/jb.00396-12

Cited by 43 publications

(38 citation statements)

References 24 publications

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“…Recently, the hypothetical protein YqjD of E. coli was characterized as a membrane-integrated ribosome-binding protein (Yoshida et al, 2012). YqjD is expressed during the stationary phase and expression is controlled by the stationary-phase sigma r S .…”

Section: Other Factors Binding Ribosomes Under Stationary Phase Stressmentioning

confidence: 99%

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The bacterial translation stress response

et al. 2014

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Throughout their life, bacteria need to sense and respond to environmental stress. Thus, such stress responses can require dramatic cellular reprogramming, both at the transcriptional as well as the translational level. This review focuses on the protein factors that interact with the bacterial translational apparatus in order to respond to and cope with different types of environmental stress. For example, the stringent factor RelA interacts with the ribosome to generate ppGpp under nutrient deprivation, whereas a variety of factors have been identified that bind to the ribosome under unfavorable growth conditions to shut-down (RelE, pY, RMF, HPF and EttA) or re-program (MazF, EF4 and BipA) translation. Additional factors have been identified that rescue ribosomes stalled due to stress-induced mRNA truncation (tmRNA, ArfA, ArfB), translation of unfavorable protein sequences (EF-P), heat shock induced subunit dissociation (Hsp15) or antibiotic inhibition (TetM, FusB). Understanding the mechanism of how the bacterial cell responds to stress will not only provide fundamental insight into translation regulation, but will also be an important step to identifying new targets for the development of novel antimicrobial agents.

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Section: Other Factors Binding Ribosomes Under Stationary Phase Stressmentioning

confidence: 99%

“…Overexpression of YqjD causes inhibition of cell growth. It has been suggested that YqjD inhibits ribosomal activity and localizes ribosomes to the membrane during stationary phase (Yoshida et al, 2012).…”

Section: Other Factors Binding Ribosomes Under Stationary Phase Stressmentioning

confidence: 99%

The bacterial translation stress response

et al. 2014

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“…Putative binding sites of some other regulators including RpoD and RpoH are also found in the promoter region of elaB, suggesting that ElaB might be involved in other stress responses. To date, three C-tail anchored inner membrane proteins, YqjD, YgaM and ElaB, have been identified in E. coli (Yoshida et al, 2012). Expression of these three genes is all induced when cells enter the stationary phase (Yoshida et al, 2012); moreover, YqjD and ElaB are not produced in the absence of RpoS.…”

Section: Discussionmentioning

confidence: 99%

“…To date, three C-tail anchored inner membrane proteins, YqjD, YgaM and ElaB, have been identified in E. coli (Yoshida et al, 2012). Expression of these three genes is all induced when cells enter the stationary phase (Yoshida et al, 2012); moreover, YqjD and ElaB are not produced in the absence of RpoS. YqjD binds to ribosomes at the N-terminal region and may cause a functional defect in the translational activity of ribosomes (Yoshida et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

Resistance to oxidative stress by inner membrane protein ElaB is regulated by OxyR and RpoS

Guo

Zhan

et al. 2019

Microbial Biotechnology

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Summary C‐tail anchored inner membrane proteins are a family of proteins that contain a C‐terminal transmembrane domain but lack an N‐terminal signal sequence for membrane targeting. They are widespread in eukaryotes and prokaryotes and play critical roles in membrane traffic, apoptosis and protein translocation in eukaryotes. Recently, we identified and characterized in Escherichia coli a new C‐tail anchored inner membrane, ElaB, which is regulated by the stationary phase sigma factor RpoS. ElaB is important for resistance to oxidative stress but the exact mechanism is unclear. Here, we show that ElaB functions as part of the adaptive oxidative stress response by maintaining membrane integrity. Production of ElaB is induced by oxidative stress at the transcriptional level. Moreover, elaB expression is also regulated by the key regulator OxyR via an OxyR binding site in the promoter of elaB . OxyR induces the expression of elaB in the exponential growth phase, while excess OxyR reduces elaB expression in an RpoS‐dependent way in the stationary phase. In addition, deletion of elaB reduced fitness compared to wild‐type cells after prolonged incubation. Therefore, we determined how ElaB is regulated under oxidative stress: RpoS and OxyR coordinately control the expression of inner membrane protein ElaB.

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“…EsaR was shown to repress production of OsmY in previous proteomic studies (13). ElaB, another protein thought to be in the S regulon, is an inner membrane protein associated with the ribosomes whose function is unknown (33). Interestingly, elaB expression is under regulation by QS in another plant-associated microbe.…”

Section: Figmentioning

confidence: 99%

Transcriptome-Based Analysis of the Pantoea stewartii Quorum-Sensing Regulon and Identification of EsaR Direct Targets

Ramachandran

Burke

Cormier

et al. 2014

Appl Environ Microbiol

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b Pantoea stewartii subsp. stewartii is a proteobacterium that causes Stewart's wilt disease in corn plants. The bacteria form a biofilm in the xylem of infected plants and produce capsule that blocks water transport, eventually causing wilt. At low cell densities, the quorum-sensing (QS) regulatory protein EsaR is known to directly repress expression of esaR itself as well as the genes for the capsular synthesis operon transcription regulator, rcsA, and a 2,5-diketogluconate reductase, dkgA. It simultaneously directly activates expression of genes for a putative small RNA, esaS, the glycerol utilization operon, glpFKX, and another transcriptional regulator, lrhA. At high bacterial cell densities, all of this regulation is relieved when EsaR binds an acylated homoserine lactone signal, which is synthesized constitutively over growth. QS-dependent gene expression is critical for the establishment of disease in the plant. However, the identity of the full set of genes controlled by EsaR/QS is unknown. A proteomic approach previously identified around 30 proteins in the QS regulon. In this study, a whole-transcriptome, next-generation sequencing analysis of rRNA-depleted RNA from QS-proficient and -deficient P. stewartii strains was performed to identify additional targets of EsaR. EsaR-dependent transcriptional regulation of a subset of differentially expressed genes was confirmed by quantitative reverse transcription-PCR (qRT-PCR). Electrophoretic mobility shift assays demonstrated that EsaR directly bound 10 newly identified target promoters. Overall, the QS regulon of P. stewartii orchestrates three major physiological responses: capsule and cell envelope biosynthesis, surface motility and adhesion, and stress response.

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YqjD Is an Inner Membrane Protein Associated with Stationary-Phase Ribosomes in Escherichia coli

Cited by 43 publications

References 24 publications

The bacterial translation stress response

The bacterial translation stress response

Resistance to oxidative stress by inner membrane protein ElaB is regulated by OxyR and RpoS

Transcriptome-Based Analysis of the Pantoea stewartii Quorum-Sensing Regulon and Identification of EsaR Direct Targets

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