Analysis of functional domains present in the N-terminus of the SipB protein

Kim, Bae Hoon; Kim, Hyeon Guk; Kim, Jin Seok; Jang, Jung Im; Park, Yong Keun

doi:10.1099/mic.0.2007/007872-0

Cited by 29 publications

(24 citation statements)

References 47 publications

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“…Central or C-terminal regions of T3S substrates were also shown to contribute to the secretion of the effector protein SipB from Salmonella spp. and the translocon protein EspB from enterohemorrhagic E. coli (93,271). As an alternative to the amino acid-based T3S signal, a signal in the corresponding mRNAs of several effector proteins from Yersinia was proposed, suggesting a cotranslational secretion of these proteins (16,17).…”

Section: Recognition Of Secreted Proteins T3s Signals Are Not Conservmentioning

confidence: 99%

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

Büttner

2012

Microbiol Mol Biol Rev

362

482

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SUMMARY Flagellar and translocation-associated type III secretion (T3S) systems are present in most Gram-negative plant- and animal-pathogenic bacteria and are often essential for bacterial motility or pathogenicity. The architectures of the complex membrane-spanning secretion apparatuses of both systems are similar, but they are associated with different extracellular appendages, including the flagellar hook and filament or the needle/pilus structures of translocation-associated T3S systems. The needle/pilus is connected to a bacterial translocon that is inserted into the host plasma membrane and mediates the transkingdom transport of bacterial effector proteins into eukaryotic cells. During the last 3 to 5 years, significant progress has been made in the characterization of membrane-associated core components and extracellular structures of T3S systems. Furthermore, transcriptional and posttranscriptional regulators that control T3S gene expression and substrate specificity have been described. Given the architecture of the T3S system, it is assumed that extracellular components of the secretion apparatus are secreted prior to effector proteins, suggesting that there is a hierarchy in T3S. The aim of this review is to summarize our current knowledge of T3S system components and associated control proteins from both plant- and animal-pathogenic bacteria.

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Section: Recognition Of Secreted Proteins T3s Signals Are Not Conservmentioning

confidence: 99%

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

Büttner

2012

Microbiol Mol Biol Rev

362

482

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“…While most effector proteins have one N-terminal secretion signal, other substrate classes appear to have additional export signals: the Yersinia ruler protein features a central stretch that is also required for export [183], and translocators as well as some effectors were shown to require both N-and C-terminal signals [184][185][186].…”

Section: Export Signalsmentioning

confidence: 99%

Type III secretion systems: the bacterial flagellum and the injectisome

Diepold

Armitage

2015

Phil. Trans. R. Soc. B

184

175

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One contribution of 12 to a theme issue 'The bacterial cell envelope'. The flagellum and the injectisome are two of the most complex and fascinating bacterial nanomachines. At their core, they share a type III secretion system (T3SS), a transmembrane export complex that forms the extracellular appendages, the flagellar filament and the injectisome needle. Recent advances, combining structural biology, cryo-electron tomography, molecular genetics, in vivo imaging, bioinformatics and biophysics, have greatly increased our understanding of the T3SS, especially the structure of its transmembrane and cytosolic components, the transcriptional, post-transcriptional and functional regulation and the remarkable adaptivity of the system. This review aims to integrate these new findings into our current knowledge of the evolution, function, regulation and dynamics of the T3SS, and to highlight commonalities and differences between the two systems, as well as their potential applications.

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“…All three methods agreed in categorizing 10 of the effectors, including InvJ and SipB, as sequence order dependent. These effectors are both SOD members and have small, well-defined sequences that are necessary for secretion (31,63), indicating that they are indeed sequence order dependent. Additionally, we have generated two randomly scrambled variants of the SseJ secretion signal that were predicted with high (SseJ-H) and low (SseJ-L) SIEVE scores (8).…”

Section: Is the Type III Secretion Signal Dependent On Order Of Aminomentioning

confidence: 99%

Computational Prediction of Type III and IV Secreted Effectors in Gram-Negative Bacteria

et al. 2011

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In this review, we provide an overview of the methods employed in four recent studies that described novel methods for computational prediction of secreted effectors from type III and IV secretion systems in Gramnegative bacteria. We present the results of these studies in terms of performance at accurately predicting secreted effectors and similarities found between secretion signals that may reflect biologically relevant features for recognition. We discuss the Web-based tools for secreted effector prediction described in these studies and announce the availability of our tool, the SIEVE server (http://www.sysbep.org/sieve). Finally, we assess the accuracies of the three type III effector prediction methods on a small set of proteins not known prior to the development of these tools that we recently discovered and validated using both experimental and computational approaches. Our comparison shows that all methods use similar approaches and, in general, arrive at similar conclusions. We discuss the possibility of an order-dependent motif in the secretion signal, which was a point of disagreement in the studies. Our results show that there may be classes of effectors in which the signal has a loosely defined motif and others in which secretion is dependent only on compositional biases. Computational prediction of secreted effectors from protein sequences represents an important step toward better understanding the interaction between pathogens and hosts.

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Analysis of functional domains present in the N-terminus of the SipB protein

Cited by 29 publications

References 47 publications

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

Type III secretion systems: the bacterial flagellum and the injectisome

Computational Prediction of Type III and IV Secreted Effectors in Gram-Negative Bacteria

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