<i>Agrobacterium</i>
            VirD2 protein interacts with plant host cyclophilins

Deng, Wanyin; Chen, Lishan; Wood, Derek W.; Metcalfe, Tracee L.; Liang, Xueya; Gordon, Milton P.; Comai, Luca; Nester, Eugene W.

doi:10.1073/pnas.95.12.7040

Cited by 102 publications

(85 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…For example, VirD2 binds three members of the Arabidopsis cyclophilin chaperone family; these interactions might maintain the proper conformation of VirD2 in the host-cell cytoplasm or nucleus during T-complex transit 79 . VirD2 also interacts with a serine/threonine phosphatase (PP2C) and, correspondingly, there is evidence for VirD2 phosphorylation in plant tissues.…”

Section: A Tumefaciens T-dna and Effector Protein Transfermentioning

confidence: 99%

The versatile bacterial type IV secretion systems

Cascales¹,

Christie²

2003

Nat Rev Microbiol

601

559

View full text Add to dashboard Cite

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...

show abstract

Section: A Tumefaciens T-dna and Effector Protein Transfermentioning

confidence: 99%

The versatile bacterial type IV secretion systems

Cascales¹,

Christie²

2003

Nat Rev Microbiol

601

559

View full text Add to dashboard Cite

show abstract

“…AtCYP18-3 was shown to interact with Agrobacterium VirD2, an endonuclease covalently bound to the 59 end of the T-DNA. Because T-DNA transfer is inhibited by CsA, CYP interaction with VirD2 may be important for agrobacterial infection (Deng et al, 1998). AtCYP26-1 is another CYP predicted to be cytosolic.…”

Section: Genomic Organization and Phylogenetic Relationship Of Arabidmentioning

confidence: 99%

“…A cyclophilin 40 homolog has been shown to regulate development of leaf shape in Arabidopsis (Berardini et al, 2001). Several plant cyclophilins interact with an endonuclease involved in T-DNA transfer from agrobacterium to host plant cells (Deng et al, 1998). Disruption of AtFKBP42 gene function caused developmental defect (Kamphausen et al, 2002).…”

mentioning

confidence: 99%

Immunophilins and Parvulins. Superfamily of Peptidyl Prolyl Isomerases in Arabidopsis

2004

View full text Add to dashboard Cite

Immunophilins are defined as receptors for immunosuppressive drugs including cyclosporin A, FK506, and rapamycin. The cyclosporin A receptors are referred to as cyclophilins (CYPs) and FK506-and rapamycin-binding proteins are abbreviated as FKBPs. These two groups of proteins (collectively called immunophilins) share little sequence homology, but both have peptidyl prolyl cis/trans isomerase (PPIase) activity that is involved in protein folding processes. Studies have identified immunophilins in all organisms examined including bacteria, fungi, animals, and plants. Nevertheless, the physiological function of immunophilins is poorly understood in any organism. In this study, we have surveyed the genes encoding immunophilins in Arabidopsis genome. A total of 52 genes have been found to encode putative immunophilins, among which 23 are putative FKBPs and 29 are putative CYPs. This is by far the largest immunophilin family identified in any organism. Both FKBPs and CYPs can be classified into single domain and multiple domain members. The single domain members contain a basic catalytic domain and some of them have signal sequences for targeting to a specific organelle. The multiple domain members contain not only the catalytic domain but also defined modules that are involved in protein-protein interaction or other functions. A striking feature of immunophilins in Arabidopsis is that a large fraction of FKBPs and CYPs are localized in the chloroplast, a possible explanation for why plants have a larger immunophilin family than animals. Parvulins represent another family of PPIases that are unrelated to immunophilins in protein sequences and drug binding properties. Three parvulin genes were found in Arabidopsis genome. The expression of many immunophilin and parvulin genes is ubiquitous except for those encoding chloroplast members that are often detected only in the green tissues. The large number of genes and diversity of structure domains and cellular localization make PPIases a versatile superfamily of proteins that clearly function in many cellular processes in plants.Immunosuppressive drugs cyclosporin A (CsA), FK506, and rapamycin are used clinically in transplantation to prevent graft rejection. During the course to understand the molecular mechanisms of immunosuppression by CsA, FK506, and rapamycin, the cellular receptors of these drugs have been purified and characterized (Schreiber, 1991;Fruman et al., 1994). CsA binds to a family of receptors named cyclophilins (CyPs), and FK506 and rapamycin bind to a distinct set of receptors called FKBPs (FK506 and rapamycin-binding proteins). Cyclophilins and FKBPs are collectively referred to as immunophilins (Schreiber, 1991).The complexes formed by immunophilins and their cognate ligands are the functional modules for immunosuppression. The FKBP12-FK506 and CyPCsA complexes, but not their separate components, bind to and inhibit the activity of calcineurin, a Ca 21 , calmodulin-dependent protein phosphatase (Liu et al., 1991). Studies have demonstrated that inhib...

show abstract

“…Other plant proteins that were identified to interact with VirD2 include several cyclophilins, a kinase CAK2M, and a protein phosphatase 2C (PP2C). Deng et al (1998) showed that an Arabdopsis cyclophilin interacted strongly with VirD2. They further characterized the interaction domain of VirD2 and found that a central domain of VirD2 (residues 274~337) was involved in the interaction with cyclophilin.…”

Section: Plant Proteins Involved In T-complex Nuclear Targetingmentioning

confidence: 99%