New features of the cell wall of the radio-resistant bacterium Deinococcus radiodurans

Farci, Domenica; Bowler, Matthew W.; Kirkpatrick, Joanna; McSweeney, Seán; Tramontano, Enzo; Piano, Dario

doi:10.1016/j.bbamem.2014.02.014

Cited by 49 publications

(82 citation statements)

References 30 publications

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“…More than 50 proteins were identified in the peeling envelope of ∆DR_146T (Table 2), and a number of proteins detected in the culture’s supernatant were also found in the peeling envelope fraction. However, some proteins were exclusive to the peeling envelope fraction, including SlpA, the putative outer membrane protein BamA (DR_0379) and the secretin (DR_0774)31. SlpA was one of the most abundant proteins in the peeling fraction but was absent in the culture’s supernatant, possibly due to the presence of its SLH domain which keeps it anchored to the outer membrane3235.…”

Section: Resultsmentioning

confidence: 99%

“…8, adapted from previous reports28313637. DR_146T might function as a TamB-like protein, anchored in the inner membrane with its N-terminal transmembrane helix and spanning the peptidoglycan and periplasm, based on the topology of TamB in E. coli 11.…”

Section: Discussionmentioning

confidence: 99%

“…The SlpA (DR_2577) is the pivotal component of the S-layer of D. radiodurans . Knockout of SlpA results in the dissociation of the S-layer core structure and consequently leads to cell envelope damage283132. Acosta and colleagues reported that SlpA of Thermus thermophilus , a bacterium evolutionally close to D. radiodurans , was assembled with assistance from the BAM complex33.…”

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A tamB homolog is involved in maintenance of cell envelope integrity and stress resistance of Deinococcus radiodurans

Dai

et al. 2017

Sci Rep

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The translocation and assembly module (TAM) in bacteria consists of TamA and TamB that form a complex to control the transport and secretion of outer membrane proteins. Herein, we demonstrated that the DR_1462-DR_1461-DR_1460 gene loci on chromosome 1 of Deinococcus radiodurans, which lacks tamA homologs, is a tamB homolog (DR_146T) with two tamB motifs and a DUF490 motif. Mutation of DR_146T resulted in cell envelope peeling and a decrease in resistance to shear stress and osmotic pressure, as well as an increase in oxidative stress resistance, consistent with the phenotype of a surface layer (S-layer) protein SlpA (DR_2577) mutant, demonstrating the involvement of DR_146T in maintenance of cell envelope integrity. The 123 kDa SlpA was absent and only its fragments were present in the cell envelope of DR_146T mutant, suggesting that DR_146T might be involved in maintenance of the S-layer. A mutant lacking the DUF490 motif displayed only a slight alteration in phenotype compared with the wild type, suggesting DUF490 is less important than tamB motif for the function of DR_146T. These findings enhance our understanding of the properties of the multilayered envelope in extremophilic D. radiodurans, as well as the diversity and functions of TAMs in bacteria.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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A tamB homolog is involved in maintenance of cell envelope integrity and stress resistance of Deinococcus radiodurans

Dai

et al. 2017

Sci Rep

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“…Also of note, BamA from the Deinococcus-Thermus phylum, which also clustered in the predominantly cyanobacterial group (BamA4 in Table S1 ), have POTRA P1 domains with strong similarity to the sequence features of the POTRA P2 domain from the FhaC protein subfamily ( Figure 4 ). These distinguishing features indicate an adapted function of the BamA of this Phylum, perhaps to unique features of their cell envelope (Farci et al, 2014). …”

Section: Resultsmentioning

confidence: 99%

A comprehensive analysis of the Omp85/TpsB protein superfamily structural diversity, taxonomic occurrence, and evolution

2014

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Members of the Omp85/TpsB protein superfamily are ubiquitously distributed in Gram-negative bacteria, and function in protein translocation (e.g., FhaC) or the assembly of outer membrane proteins (e.g., BamA). Several recent findings are suggestive of a further level of variation in the superfamily, including the identification of the novel membrane protein assembly factor TamA and protein translocase PlpD. To investigate the diversity and the causal evolutionary events, we undertook a comprehensive comparative sequence analysis of the Omp85/TpsB proteins. A total of 10 protein subfamilies were apparent, distinguished in their domain structure and sequence signatures. In addition to the proteins FhaC, BamA, and TamA, for which structural and functional information is available, are families of proteins with so far undescribed domain architectures linked to the Omp85 β-barrel domain. This study brings a classification structure to a dynamic protein superfamily of high interest given its essential function for Gram-negative bacteria as well as its diverse domain architecture, and we discuss several scenarios of putative functions of these so far undescribed proteins.

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“…Recently, Farci et al (2014) detected two peptidases associated to the cell wall of D. radiodurans that had been predicted by the genes DR_2310 and DR_A0283. According to White et al (1999), an uncharacterized peptidase from the catalytic domain of metallopeptidases (DR_2310) was described with a molecular mass of 84.2 kDa and a probable subtilase-type serine protease (DR_A0283) was described with a molecular mass of 76.6 kDa.…”

Section: Discussionmentioning

confidence: 99%

Extracellular peptidases from Deinococcus radiodurans

et al. 2015

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The extremophile Deinococcus radiodurans wild type R1 produces peptidases (metallo- and serine-) in TGY medium and in the media supplemented with human hair (HMY) and chicken feathers (FMY). Enzymatic screening on agar plates revealed peptidase activity. In TGY medium metallopeptidases were detected corresponding to a molecular mass range of 300-85 kDa (gelatinases); 280-130 (caseinases) and a 300 and a 170 kDa (keratinases); and a gelatinolytic serine peptidase (75 kDa). In HMY medium after 144 h, D. radiodurans produced keratinase (290 U/ml), gelatinase (619 U/ml) and sulfite (26 µg/ml). TGY medium produced higher proteolytic activity: 950 U/ml of gelatinolytic (24 h); 470 U/ml of keratinolytic (24 h) and 110 U/ml of caseinolytic (72 h). In the FMY medium, we found gelatinolytic (317 U/ml), keratinolytic (43 U/ml) and caseinolytic (85 U/ml) activities. The sulfite had a maximum release at 48 h (8.1 µg/ml). Enzymography analysis revealed that the keratinases degraded keratin after 24 h of reaction. The addition of sodium sulfite (1.0 %) improved the keratin degradation. Environmental Scanning Electron microscopy revealed alterations such as damage and holes in the hair fiber cuticle after D. radiodurans growth. This work presents for the first time D. radiodurans as a new keratinolytic microorganism.

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New features of the cell wall of the radio-resistant bacterium Deinococcus radiodurans

Cited by 49 publications

References 30 publications

A tamB homolog is involved in maintenance of cell envelope integrity and stress resistance of Deinococcus radiodurans

A tamB homolog is involved in maintenance of cell envelope integrity and stress resistance of Deinococcus radiodurans

A comprehensive analysis of the Omp85/TpsB protein superfamily structural diversity, taxonomic occurrence, and evolution

Extracellular peptidases from Deinococcus radiodurans

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