The
            <i>Tn7</i>
            transposition regulator TnsC interacts with the transposase subunit TnsB and target selector TnsD

Choi, Ki Young; Spencer, Jeanelle M.; Craig, Nancy L.

doi:10.1073/pnas.1409869111

Cited by 43 publications

(36 citation statements)

References 38 publications

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“…Extensive studies on the Mu transposase have revealed that the ATPase subunit MuB associates with the RNase H fold ( 74 ) endoDNase subunit MuA that cuts the target DNA for transposition ( 75 , 76 ). Similar studies on the TN7 transposase have revealed that its ATPase subunit TnsC associates with two subunits, TnsA and TnsB, which contain REase and RNase H fold endoDNase domains, respectively ( 71 , 77 ). In both Mu and TN7 the ATP-bound STAND ATPase is required for association with the target DNA and activates the endoDNase subunits to cut the donor DNA ( 78 , 79 ).…”

Section: Resultsmentioning

confidence: 68%

Transposons to toxins: the provenance, architecture and diversification of a widespread class of eukaryotic effectors

et al. 2016

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Enzymatic effectors targeting nucleic acids, proteins and other cellular components are the mainstay of conflicts across life forms. Using comparative genomics we identify a large class of eukaryotic proteins, which include effectors from oomycetes, fungi and other parasites. The majority of these proteins have a characteristic domain architecture with one of several N-terminal ‘Header’ domains, which are predicted to play a role in trafficking of these effectors, including a novel version of the Ubiquitin fold. The Headers are followed by one or more diverse C-terminal domains, such as restriction endonuclease (REase), protein kinase, HNH endonuclease, LK-nuclease (a RNase) and multiple distinct peptidase domains, which are predicted to carry their toxicity determinants. The most common types of these proteins appear to have originated from prokaryotic transposases (e.g. TN7 and Mu) and combine a CDC6/ORC1-STAND clade NTPase domain with a C-terminal REase domain. Other than the so-called Crinkler effectors of oomycetes and fungi, these effectors are encoded by other eukaryotic parasites such as trypanosomatids (the RHS proteins) and the rhizarian Plasmodiophora, and symbionts like Capsaspora. Remarkably, we also find these proteins in free-living eukaryotes, including several viridiplantae, fungi, amoebozoans and animals. These versions might either still be transposons or function in other poorly understood eukaryote-specific inter-organismal and inter-genomic conflicts. These include the Medea1 selfish element of Tribolium that spreads via post-zygotic killing. We present a unified mechanism for the recombination-dependent diversification and action of this widespread class of molecular weaponry deployed across diverse conflicts ranging from parasitic to free-living forms.

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Section: Resultsmentioning

confidence: 68%

Transposons to toxins: the provenance, architecture and diversification of a widespread class of eukaryotic effectors

et al. 2016

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“…We thus employed a systematic in vivo photo‐cross‐linking approach to identify possible interacting partners in an unbiased manner (Chin et al ., ; Chin and Schultz, ). This technique has been successfully applied to analysis of protein–protein interactions in a variety of biological processes (Mori and Ito, ; Freinkman et al ., ; Choi et al ., ; Shiota et al ., ; Maklashina et al ., ; Miyazaki et al ., ; Akiyama et al ., ). Each codon for the 179 residues in the entire TPR domain (309–487) was changed to an amber codon by site‐directed mutagenesis to allow suppressor tRNA‐mediated incorporation of a nonnatural, photoreactive amino acid, p ‐benzoylphenylalanine (pBPA).…”

Section: Resultsmentioning

confidence: 97%

The TPR domain of BepA is required for productive interaction with substrate proteins and the β‐barrel assembly machinery complex

Daimon

Iwama-Masui

Tanaka

et al. 2017

Molecular Microbiology

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BepA (formerly YfgC) is an Escherichia coli periplasmic protein consisting of an N-terminal protease domain and a C-terminal tetratricopeptide repeat (TPR) domain. We have previously shown that BepA is a dual functional protein with chaperone-like and proteolytic activities involved in membrane assembly and proteolytic quality control of LptD, a major component of the outer membrane lipopolysaccharide translocon. Intriguingly, BepA can associate with the BAM complex: the β-barrel assembly machinery (BAM) driving integration of β-barrel proteins into the outer membrane. However, the molecular mechanism of BepA function and its association with the BAM complex remains unclear. Here, we determined the crystal structure of the BepA TPR domain, which revealed the presence of two subdomains formed by four TPR motifs. Systematic site-directed in vivo photo-cross-linking was used to map the protein-protein interactions mediated by the BepA TPR domain, showing that this domain interacts both with a substrate and with the BAM complex. Mutational analysis indicated that these interactions are important for the BepA functions. These results suggest that the TPR domain plays critical roles in BepA functions through interactions both with substrates and with the BAM complex. Our findings provide insights into the mechanism of biogenesis and quality control of the outer membrane.

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“…In multidrug-resistant Enterobacteriaceae bacteria, Tn7-like transposons play a very vital role due to their high capability for transferring antimicrobial resistance genes (37). Through drug susceptibility tests, we found that the multi-drug resistance of Enterobacteriaceae carrying Tn7-like is widespread in various strains.…”

Section: Discussionmentioning

confidence: 92%

Characterization of Tn7-like transposons and its related antibiotic resistance among Enterobacteriaceae from livestock and poultry in China

He¹,

Li²,

Cui³

et al. 2020

Preprint

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Background: This study was aimed to investigate the prevalence and structure of Tn7-like in Enterobacteriaceae from livestock and poultry as well as their possible role as reservoir of antibiotic resistance genes (ARGs). Methods:Polymerase chain reaction (PCR) and DNA sequencing analyses were used for the characterization of Tn7-like, associated integrons and ARGs. The antimicrobial resistance profile of the isolates was examined by using disc diffusion test.Results: Three hundred and seventy-eight Tn7-like-positive strains of Enterobacteriaceae were isolated, and included E. coli (128), Proteus(150), K. pneumonia(17), Salmonella(13), M. morganii (21) and A. baumannii(1), wherein high resistance was observed for Trimethoprim/Sulfamethoxazole and Streptomycin, and fifty percent of the strains were multidrug-resistant. Integrons class 2 were detected in all of the isolates and there are high frequency mutation sites especially in 535, a stop mutation. Variable region of class 2 integrons carried same gene cassettes, namely aadA1-sat2-dfrA1.From the 378 isolated strains, we found a new type of Tn7-like on a plasmid, named Tn6765. Conclusions:These findings proved that the Tn7-like can contribute to the horizontal transmission of antibiotic resistant genes in livestock and poultry. As potential vessels for antibiotic resistance genes (ARGs), Tn7-like could not be ignored due to their efficient transfer ability in environments.

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The Tn7 transposition regulator TnsC interacts with the transposase subunit TnsB and target selector TnsD

Cited by 43 publications

References 38 publications

Transposons to toxins: the provenance, architecture and diversification of a widespread class of eukaryotic effectors

Transposons to toxins: the provenance, architecture and diversification of a widespread class of eukaryotic effectors

The TPR domain of BepA is required for productive interaction with substrate proteins and the β‐barrel assembly machinery complex

Characterization of Tn7-like transposons and its related antibiotic resistance among Enterobacteriaceae from livestock and poultry in China

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