Regulation of a
            <i>Bacillus subtilis</i>
            mobile genetic element by intercellular signaling and the global DNA damage response

Auchtung, Jennifer M.; Lee, Catherine A.; Monson, Rita E.; Lehman, Alisa P.; Grossman, Alan D.

doi:10.1073/pnas.0505835102

Cited by 246 publications

(548 citation statements)

References 47 publications

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“…CwlT has a putative signal peptide (from aa 1 to 22, black box), an SLT domain (from aa 62 to 164, light gray box) (actually this domain is a muramidase domain), and an NlpC/P60 domain (from aa 216 to 328, dark gray box). Although yddFGIJ and cwlT were previously predicted as prophage genes (22), they are now genes in ICE (23). The arrow indicates a putative terminator (Ϫ23.7 kcal/mol).…”

Section: Resultsmentioning

confidence: 99%

“…However, this region was recently determined to be an integrative and conjugative element, ICEBs1 (23). Tn916 is the best characterized ICE (35), and orf14 in it comprising 333 amino acid residues (36) exhibits very high sequence similarity with the entire region of CwlT (43% identity; from 13 aa to 329).…”

Section: Discussionmentioning

confidence: 99%

“…Recently this region was determined to be an integrative and conjugative element, ICEBs1 (23). To analyze the expression of cwlT, a cwlT-lacZ transcriptional fusion gene was constructed, and the transcription of cwlT was determined as ␤-galactosidase activity.…”

Section: Fvl2cmentioning

confidence: 99%

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Identification and Characterization of Novel Cell Wall Hydrolase CwlT

Fukushima

Kitajima

Yamaguchi

et al. 2008

Journal of Biological Chemistry

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A cell wall hydrolase homologue, Bacillus subtilis YddH (renamed CwlT), was determined to be a novel cell wall lytic enzyme. The cwlT gene is located in the region of an integrative and conjugative element (ICEBs1), and a cwlT-lacZ fusion experiment revealed the significant expression when mitomycin C was added to the culture. Judging from the Pfam data base, CwlT (cell wall lytic enzyme T (Two-catalytic domains)) has two hydrolase domains that exhibit high amino acid sequence similarity to DL-endopeptidases and relatively low similarity to lytic transglycosylases at the C and N termini, respectively. The purified C-terminal domain of CwlT (CwlT-C-His) could hydrolyze the linkage of D-␥-glutamyl-meso-diaminopimelic acid in B. subtilis peptidoglycan, suggesting that the C-terminal domain acts as a DL-endopeptidase. On the other hand, the purified N-terminal domain (CwlT-N-His) could also hydrolyze the peptidoglycan of B. subtilis. However, on reverse-phase HPLC and mass spectrometry (MS) and MS-MS analyses of the reaction products by CwlT-N-His, this domain was determined to act as an N-acetylmuramidase and not a lytic transglycosylase. Moreover, the site-directed mutagenesis analysis revealed that Glu-87 and Asp-94 are sites related with the cell wall lytic activity. Because the amino acid sequence of the N-terminal domain of CwlT exhibits low similarity compared with those of the soluble lytic transglycosylase and muramidase (goose lysozyme), this domain represents "a new category of cell wall hydrolases."Many microorganisms have peptidoglycan as a major component of the cell wall, which consists of glycan strands crosslinked by peptides. Bacteria have various cell wall lytic enzymes. For Bacillus subtilis, more than 30 candidate peptidoglycan hydrolases are proposed on the basis of amino acid sequence similarity (1), and these enzymes are important in various cellular processes during vegetative growth, sporulation, and germination (1, 2). Several groups of peptidoglycan hydrolases are enzymatically identified as follows: N-acetylglucosaminidases (digesting GlcNAc-MurNAc 3 linkage), N-acetylmuramoyl-Lalanine amidases (digesting MurNAc-L-alanine linkage), DL-endopeptidases (digesting D-glutamic acid-meso-A 2 pm linkage) (1, 2), and LD-endopeptidase (digesting L-alanine-D-glutamic acid linkage) (3). However, the characterization of the group of DD-endopeptidase (digesting the cross-linked D-alanine-meso-A 2 pm linkage) has not been reported in B. subtilis. Interestingly, the groups of muramidase and lytic transglycosylase (digesting MurNAc-GlcNAc linkage) in B. subtilis are still not characterized, even many hydrolases in those groups, including hen egg white lysozyme, have already been identified.Previously Atrih et al. (4) described that the vegetative peptidoglycan in B. subtilis includes (136)-anhydro-N-acetylmuramic acid. Thus, it is possible that lytic transglycosylase, which digests MurNAc-GlcNAc linkage with synthesis of a 1,6-anhydro bond in the N-acetylmuramic acid (5), hydrolyzes the vegetative peptid...

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Identification and Characterization of Novel Cell Wall Hydrolase CwlT

Fukushima

Kitajima

Yamaguchi

et al. 2008

Journal of Biological Chemistry

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“…However it is possible that such elements could help the transfer process of the ICEs acting as triggers for the activation of the damage-repair machinery found in the host cells. It has already been suggested that the damage-repair machinery is important for the integration of the ICEs in the chromosome of the host cells (Auchtung et al, 2005).…”

Section: General Characteristicsmentioning

confidence: 99%

Molecular analysis of an integrative conjugative element, ICEH, present in the chromosome of different strains of Mycoplasma hyopneumoniae

et al. 2007

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Diversification of bacterial species and pathotypes is largely caused by lateral gene transfer (LGT) of diverse mobile DNA elements such as plasmids, phages, transposons and genomic islands. Thus, acquisition of new phenotypes by LGT is very important for bacterial evolution and relationship with hosts. This paper reports a 23 kb region containing fourteen CDSs with similarity to the previous described Integrative Conjugal Element of Mycoplasma fermentans (ICEF). This element, named ICEH, is present as one copy at distinct integration sites in the chromosome of 7448 and 232 pathogenic strains and is absent in the type strain J (non-pathogenic). Notable differences in the nucleotide composition of the insertion sites were detected, and could be correlated to a lack of specificity of the ICEH integrase. Although present in strains of the same organism, the ICEH elements are more divergent than the typical similarity between other chromosomal locus of Mycoplasma hyopneunomiae, suggesting an accelerated evolution of these constins or an ongoing process of degeneration, while maintaining conservation of the tra genes. An extrachromosomal form of this element had been detected in the 7448 strain, suggesting a possible involvement in its mobilization and transference of CDSs to new hosts.

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“…ICEBs1 has a phage-like tyrosine recombinase and excises at a higher rate upon DNA damage and in a recA-dependent manner (23). To determine if DNA damage induces the excision of ICE6013, strains JE2 and RN4220 were UV irradiated at 25 J/m 2 and 100 J/m 2 .…”

Section: Resultsmentioning

confidence: 99%

Transposase-Mediated Excision, Conjugative Transfer, and Diversity of ICE 6013 Elements in Staphylococcus aureus

et al. 2017

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ICE6013 represents one of two families of integrative conjugative elements (ICEs) identified in the pan-genome of the human and animal pathogen Staphylococcus aureus. Here we investigated the excision and conjugation functions of ICE6013 and further characterized the diversity of this element. ICE6013 excision was not significantly affected by growth, temperature, pH, or UV exposure and did not depend on recA. The IS30-like DDE transposase (Tpase; encoded by orf1 and orf2) of ICE6013 must be uninterrupted for excision to occur, whereas disrupting three of the other open reading frames (ORFs) on the element significantly affects the level of excision. We demonstrate that ICE6013 conjugatively transfers to different S. aureus backgrounds at frequencies approaching that of the conjugative plasmid pGO1. We found that excision is required for conjugation, that not all S. aureus backgrounds are successful recipients, and that transconjugants acquire the ability to transfer ICE6013. Sequencing of chromosomal integration sites in serially passaged transconjugants revealed a significant integration site preference for a 15-bp AT-rich palindromic consensus sequence, which surrounds the 3-bp target site that is duplicated upon integration. A sequence analysis of ICE6013 from different host strains of S. aureus and from eight other species of staphylococci identified seven divergent subfamilies of ICE6013 that include sequences previously classified as a transposon, a plasmid, and various ICEs. In summary, these results indicate that the IS30-like Tpase functions as the ICE6013 recombinase and that ICE6013 represents a diverse family of mobile genetic elements that mediate conjugation in staphylococci.IMPORTANCE Integrative conjugative elements (ICEs) encode the abilities to integrate into and excise from bacterial chromosomes and plasmids and mediate conjugation between bacteria. As agents of horizontal gene transfer, ICEs may affect bacterial evolution. ICE6013 represents one of two known families of ICEs in the pathogen Staphylococcus aureus, but its core functions of excision and conjugation are not well studied. Here, we show that ICE6013 depends on its IS30-like DDE transposase for excision, which is unique among ICEs, and we demonstrate the conjugative transfer and integration site preference of ICE6013. A sequence analysis revealed that ICE6013 has diverged into seven subfamilies that are dispersed among staphylococci.

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Regulation of a Bacillus subtilis mobile genetic element by intercellular signaling and the global DNA damage response

Cited by 246 publications

References 47 publications

Identification and Characterization of Novel Cell Wall Hydrolase CwlT

Identification and Characterization of Novel Cell Wall Hydrolase CwlT

Molecular analysis of an integrative conjugative element, ICEH, present in the chromosome of different strains of Mycoplasma hyopneumoniae

Transposase-Mediated Excision, Conjugative Transfer, and Diversity of ICE 6013 Elements in Staphylococcus aureus

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