Operon Required for Fruiting Body Development in Myxococcus xanthus

Kim, Do Hee; Chung, Jin Woo; Hyun, Hyesook; Lee, Cha Yul; Lee, Kyung Ho; Cho, Kyungyun

doi:10.4014/jmb.0903.0112

Cited by 5 publications

(5 citation statements)

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“…The amino acid sequence of XAC3733 shares 40% identity with XAC0208, 35% with XAC0226, 39% with XOO4483 and Smal_0123, 38% with XCC0563 and 34% with PP_5048, PA5125, VV1_0892 and AGRO_4553. Notably, the gene products in V. vulnificus (VV1_0892) and in A. tumefaciens (AGRO_4553) have already been implicated in biofilm formation (Kim et al ., 2009a,b; Ruffing and Chen, ).…”

Section: Resultsmentioning

confidence: 99%

“…The findings in this paper add to our understanding of the factors that contribute to the ability of Xcc to form mature biofilms and to pathogenesis by establishing of role for XbmR (XAC3733) in these processes. To our knowledge, this is the first description of the role of this gene in chemotaxis and biofilm formation in the genus of Xanthomonas , although previous studies in V. vulnificus have shown that an NtrC family protein is associated with biofilm formation (Kim et al ., ,). In Xcc , the defects in chemotaxis and biofilm formation in the xbmR mutant strain could both be a result of the absence of the flagellar structure which is essential for motility in the chemotaxis assay and in the development of a mature biofilm (Malamud et al ., ).…”

Section: Discussionmentioning

confidence: 99%

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XbmR, a new transcription factor involved in the regulation of chemotaxis, biofilm formation and virulence in Xanthomonas citri subsp. citri

Yaryura

Conforte

Malamud

et al. 2014

Environmental Microbiology

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Xanthomonas citri subsp. citri (Xcc) is the causal agent of citrus canker. Biofilm formation on citrus leaves plays an important role in epiphytic survival of Xcc. Biofilm formation is affected by transposon insertion in XAC3733, which encodes a transcriptional activator of the NtrC family, not linked to a gene encoding a sensor protein, thus could be considered as an 'orphan' regulator whose function is poorly understood in Xanthomonas spp. Here we show that mutation of XAC3733 (named xbmR) resulted in impaired structural development of the Xcc biofilm, loss of chemotaxis and reduced virulence in grapefruit plants. All defective phenotypes were restored to wild-type levels by the introduction of PA2567 from Pseudomonas aeruginosa, which encodes a phosphodiesterase active in the degradation of cyclic diguanosine monophosphate (c-di-GMP). A knockout of xbmR led to a substantial downregulation of fliA that encodes a σ(28) transcription factor, as well as fliC and XAC0350 which are potential member of the σ(28) regulon. XAC0350 encodes an HD-GYP domain c-di-GMP phosphodiesterase. These findings suggest that XbmR is a key regulator of flagellar-dependent motility and chemotaxis exerting its action through a regulatory pathway that involves FliA and c-di-GMP.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

XbmR, a new transcription factor involved in the regulation of chemotaxis, biofilm formation and virulence in Xanthomonas citri subsp. citri

Yaryura

Conforte

Malamud

et al. 2014

Environmental Microbiology

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“…A genetic study of M. xanthus found the EncA gene to be required for fruiting body formation, though it was not recognized as an encapsulin homolog at the time (Kim et al, 2009). Fruiting body formation is a developmental program triggered by starvation and resulting in sporulation (Zusman et al, 2007).…”

Section: Encapsulin Nanocompartment Assembly Is Induced Under Starvatmentioning

confidence: 99%

A virus capsid‐like nanocompartment that stores iron and protects bacteria from oxidative stress

et al. 2014

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Living cells compartmentalize materials and enzymatic reactions to increase metabolic efficiency. While eukaryotes use membrane-bound organelles, bacteria and archaea rely primarily on protein-bound nanocompartments. Encapsulins constitute a class of nanocompartments widespread in bacteria and archaea whose functions have hitherto been unclear. Here, we characterize the encapsulin nanocompartment from Myxococcus xanthus, which consists of a shell protein (EncA, 32.5 kDa) and three internal proteins (EncB, 17 kDa; EncC, 13 kDa; EncD, 11 kDa). Using cryo-electron microscopy, we determined that EncA self-assembles into an icosahedral shell 32 nm in diameter (26 nm internal diameter), built from 180 subunits with the fold first observed in bacteriophage HK97 capsid. The internal proteins, of which EncB and EncC have ferritin-like domains, attach to its inner surface. Native nanocompartments have dense iron-rich cores. Functionally, they resemble ferritins, cage-like iron storage proteins, but with a massively greater capacity (~30,000 iron atoms versus ~3,000 in ferritin). Physiological data reveal that few nanocompartments are assembled during vegetative growth, but they increase fivefold upon starvation, protecting cells from oxidative stress through iron sequestration.

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“…The diversity of the cargo activities in the encapsulins suggests that this compartmentalization strategy has evolved to fulfill diverse physiological roles. The multi-cargo encapsulin system of M. xanthus has been characterized in detail [31,84,85]. Through their ferroxidase activity, EncB and EncC can oxidize, mineralize, and sequester large amounts of iron and phosphorus [30,[86][87][88].…”

Section: Physiological Role Of Encapsulinsmentioning

confidence: 99%

“…Through their ferroxidase activity, EncB and EncC can oxidize, mineralize, and sequester large amounts of iron and phosphorus [30,[86][87][88]. EncA is essential for fruiting body formation [85], a starvation response that leads to sporulation [89]. The assembly of nanocompartments induced during starvation protects the cells from death due to oxidative stress caused by peroxide exposure.…”

Section: Physiological Role Of Encapsulinsmentioning

confidence: 99%

Nanotechnological Applications Based on Bacterial Encapsulins

et al. 2021

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Encapsulins are proteinaceous nanocontainers, constructed by a single species of shell protein that self-assemble into 20–40 nm icosahedral particles. Encapsulins are structurally similar to the capsids of viruses of the HK97-like lineage, to which they are evolutionarily related. Nearly all these nanocontainers encase a single oligomeric protein that defines the physiological role of the complex, although a few encapsulate several activities within a single particle. Encapsulins are abundant in bacteria and archaea, in which they participate in regulation of oxidative stress, detoxification, and homeostasis of key chemical elements. These nanocontainers are physically robust, contain numerous pores that permit metabolite flux through the shell, and are very tolerant of genetic manipulation. There are natural mechanisms for efficient functionalization of the outer and inner shell surfaces, and for the in vivo and in vitro internalization of heterologous proteins. These characteristics render encapsulin an excellent platform for the development of biotechnological applications. Here we provide an overview of current knowledge of encapsulin systems, summarize the remarkable toolbox developed by researchers in this field, and discuss recent advances in the biomedical and bioengineering applications of encapsulins.

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Operon Required for Fruiting Body Development in Myxococcus xanthus

Cited by 5 publications

References 0 publications

XbmR, a new transcription factor involved in the regulation of chemotaxis, biofilm formation and virulence in Xanthomonas citri subsp. citri

XbmR, a new transcription factor involved in the regulation of chemotaxis, biofilm formation and virulence in Xanthomonas citri subsp. citri

A virus capsid‐like nanocompartment that stores iron and protects bacteria from oxidative stress

Nanotechnological Applications Based on Bacterial Encapsulins

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