VirE2, a Type IV secretion substrate, interacts with the VirD4 transfer protein at cell poles of <i>Agrobacterium tumefaciens</i>

Atmakuri, Krishnamohan; Ding, Zhiyong; Christie, Peter J.

doi:10.1046/j.1365-2958.2003.03669.x

Cited by 134 publications

(150 citation statements)

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“…Pili are produced both on the lateral sides and on the poles of a bacterium, although in case of the A. tumefaciens T-pili they are more abundantly found at cell poles . Likewise, the Mpf transport apparatus of A. tumefaciens (VirB/VirD4) localizes to the bacterial poles (Atmakuri et al, 2003;Judd et al, 2005;Kumar and Das, 2002). This diVerence of the A. tumefaciens VirB/VirD4 system versus bacterial conjugation systems is also reXected in the observed Fig.…”

Section: The Foreplay Of Bacterial Sex: Mating Pair Formationmentioning

confidence: 61%

“…This indicates that substrate recognition by the CP primarily occurs via interactions with protein components of the transfer-competent protein/DNA-intermediate. By analogy, the CP of A. tumefaciens, VirD4, interacts with the protein substrate VirE2 (Atmakuri et al, 2003), which is secreted into plant cells independent of T-DNA transfer (Vergunst et al, 2000). The interaction is mediated by the C-terminal domain of VirE2 (Atmakuri et al, 2003).…”

Section: Cp (Vird4): the Cytoplasmic Gate To The Secretion Channelmentioning

confidence: 99%

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The mating pair formation system of conjugative plasmids—A versatile secretion machinery for transfer of proteins and DNA

Schröder

Lanka

2005

Plasmid

190

146

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The mating pair formation (Mpf) system functions as a secretion machinery for intercellular DNA transfer during bacterial conjugation. The components of the Mpf system, comprising a minimal set of 10 conserved proteins, form a membrane-spanning protein complex and a surface-exposed sex pilus, which both serve to establish intimate physical contacts with a recipient bacterium. To function as a DNA secretion apparatus the Mpf complex additionally requires the coupling protein (CP). The CP interacts with the DNA substrate and couples it to the secretion pore formed by the Mpf system. Mpf/CP conjugation systems belong to the family of type IV secretion systems (T4SS), which also includes DNA-uptake and -release systems, as well as eVector protein translocation systems of bacterial pathogens such as Agrobacterium tumefaciens (VirB/VirD4) and Helicobacter pylori (Cag). The increased eVorts to unravel the molecular mechanisms of type IV secretion have largely advanced our current understanding of the Mpf/CP system of bacterial conjugation systems. It has become apparent that proteins coupled to DNA rather than DNA itself are the actively transported substrates during bacterial conjugation. We here present a uniWed and updated view of the functioning and the molecular architecture of the Mpf/CP machinery. 

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Section: The Foreplay Of Bacterial Sex: Mating Pair Formationmentioning

confidence: 61%

Section: Cp (Vird4): the Cytoplasmic Gate To The Secretion Channelmentioning

confidence: 99%

The mating pair formation system of conjugative plasmids—A versatile secretion machinery for transfer of proteins and DNA

Schröder

Lanka

2005

Plasmid

190

146

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“…Cytological evidence favouring this role was recently presented. In A. tumefaciens, the VirD4 CP localizes at the cell poles 37 or it can be artificially localized at the mid-cell 38,39 , so marking distinct cellular positions for monitoring the recruitment of substrates tagged with green fluorescent protein (GFP). Indeed, VirD4 was shown to recruit GFP fused to the VirE2 effector protein, and further cytological and biochemical studies established that the interaction occurs independently of any requirement for Mpf proteins, the T-strand or even VirE1, a secretion CHAPERONE for VirE2 (REF.…”

Section: The Hexameric Coupling Protein: a Substrate-recruitment Factmentioning

confidence: 99%

“…Indeed, VirD4 was shown to recruit GFP fused to the VirE2 effector protein, and further cytological and biochemical studies established that the interaction occurs independently of any requirement for Mpf proteins, the T-strand or even VirE1, a secretion CHAPERONE for VirE2 (REF. 39). Of further interest, VirD4 was shown to interact with the carboxy-terminal region of VirE2, adding to evidence that SECRETION SIGNALS are localized at the carboxyl termini of VirE2 and other protein substrates of the VirB/D4 T4S system [39][40][41][42] .…”

Section: The Hexameric Coupling Protein: a Substrate-recruitment Factmentioning

confidence: 99%

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The versatile bacterial type IV secretion systems

Cascales¹,

Christie²

2003

Nat Rev Microbiol

Self Cite

600

559

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Bacteria use type IV secretion systems for two fundamental objectives related to pathogenesisgenetic exchange and the delivery of effector molecules to eukaryotic target cells. Whereas gene acquisition is an important adaptive mechanism that enables pathogens to cope with a changing environment during invasion of the host, interactions between effector and host molecules can suppress defence mechanisms, facilitate intracellular growth and even induce the synthesis of nutrients that are beneficial to bacterial colonization. Rapid progress has been made towards defining the structures and functions of type IV secretion machines, identifying the effector molecules, and elucidating the mechanisms by which the translocated effectors subvert eukaryotic cellular processes during infection. The year 2003 marks the fiftieth anniversary of the first description of a TYPE IV SECRETION (T4S)SYSTEM: the CONJUGATION apparatus of the F plasmid 1 . This is a dynamic bacterial surface organelle, the activities of which are now known to include the contact-dependent delivery of DNA to bacterial recipients and the assembly and retraction of a conjugal PILUS 2 . In the past decade, reports describing systems that are ancestrally related to the F-transfer system and other conjugation machines have emerged. Instead of mediating DNA transfer between bacteria, these systems deliver DNA or protein substrates, known as effectors, to eukaryotic target cells during infection [3][4][5] . More recently, several new T4S systems have been described that are also ancestrally related to the conjugation machines, but these systems mediate the exchange of DNA with the extracellular milieu [6][7][8] . Collectively, this diversity of function in the face of a common ancestry makes the T4S machines attractive subjects for comparative studies that explore the dynamics of organelle assembly and action. Additionally, from a medical perspective, it is of enormous interest to develop a detailed understanding of how the inter-kingdom transfer of type IV effector molecules contributes to pathogenesis. This review will summarize the recent advances in our knowledge of T4S, NIH Public Access Author ManuscriptNat Rev Microbiol. Author manuscript; available in PMC 2013 December 27. NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscriptwith an emphasis on machine structure and function, and the activities of effectors after translocation into the eukaryotic host. The T4S familyThis fascinatingly versatile translocation family can be classified into three subfamilies, each of which contributes in unique ways to pathogenesis ( Fig. 1; Table 1). The largest subfamily, the conjugation systems, are found in most species of Gram-negative and Grampositive bacteria. These systems mediate DNA transfer both within and between phylogenetically diverse species, and some systems even deliver DNA to fungi, plants and human cells 2,9-13 . Conjugation is an important contributor to genome plasticity, and therefore bacterial fitness under changing en...

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Visualization of Protein Interactions in Living Cells Using Bimolecular Fluorescence Complementation (BiFC) Analysis

Grinberg

Kerppola

2005

CP Protein Science

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Protein interactions integrate stimuli from different signaling pathways and developmental programs. Bimolecular fluorescence complementation (BiFC) analysis has been developed for visualization of protein interactions in living cells. This approach is based on complementation between two fragments of a fluorescent protein when they are brought together by an interaction between proteins fused to the fragments, and it enables visualization of the subcellular locations of protein interactions in the normal cellular environment. It can be used for the analysis of many protein interactions and does not require information about the structures of the interaction partners. A multicolor BiFC approach has been developed for simultaneous visualization of interactions with multiple alternative partners in the same cell, based on complementation between fragments of engineered fluorescent proteins that produce bimolecular fluorescent complexes with distinct spectral characteristics. This enables comparison of subcellular distributions of different protein complexes in the same cell and allows analysis of competition between mutually exclusive interaction partners.

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VirE2, a Type IV secretion substrate, interacts with the VirD4 transfer protein at cell poles of Agrobacterium tumefaciens

Cited by 134 publications

References 68 publications

The mating pair formation system of conjugative plasmids—A versatile secretion machinery for transfer of proteins and DNA

The mating pair formation system of conjugative plasmids—A versatile secretion machinery for transfer of proteins and DNA

The versatile bacterial type IV secretion systems

Visualization of Protein Interactions in Living Cells Using Bimolecular Fluorescence Complementation (BiFC) Analysis

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