Specificity and Target Proteins of Arginine-Specific Mono-ADP-Ribosylation in T-Tubules of Rabbit Skeletal Muscle

Klebl, Bert; Göpel, Sven; Pette, Dirk

doi:10.1006/abbi.1997.0330

Cited by 7 publications

(6 citation statements)

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“…To address this problem, we devised an ADPr assay that exploited an analogue of β-NAD, ethenoNAD (εNAD) (Klebl et al, 1997), in which ADPr of substrates could be monitored by Western blotting with α-ethenoadenosine (α-εAdo) (Krebs et al, 2003). To assay for SdeC ART activity directed against mammalian proteins, while simultaneously monitoring cellular ubiquitination changes in response to Sde proteins, recombinant full-length SdeC was incubated with cell extracts and recombinant HA-Ub in the presence of εNAD.…”

Section: Resultsmentioning

confidence: 99%

A Single Legionella Effector Catalyzes a Multistep Ubiquitination Pathway to Rearrange Tubular Endoplasmic Reticulum for Replication

Kotewicz

Ramabhadran

Sjoblom

et al. 2017

Cell Host & Microbe

181

267

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Summary Intracellular pathogens manipulate host organelles to support replication within cells. For Legionella pneumophila, the bacterium translocates proteins that establish an endoplasmic reticulum (ER)-associated replication compartment. We show here that the bacterial Sde proteins target host reticulon 4 (Rtn4) to control tubular ER dynamics, resulting in tubule rearrangements as well as alterations in Rtn4 associated with the replication compartment. These rearrangements are triggered via Sde-promoted ubiquitin transfer to Rtn4, occurring almost immediately after bacterial uptake. Ubiquitin transfer requires two sequential enzymatic activities from a single Sde polypeptide: an ADP-ribosyltransferase and a nucleotidase/phosphohydrolase. The ADP-ribosylated moiety of ubiquitin is a substrate for the nucleotidase/phosphohydrolase, resulting in either transfer of ubiquitin to Rtn4, or phosphoribosylation of ubiquitin in the absence of a ubiquitination target. Therefore, a single bacterial protein drives a multistep biochemical pathway to control ubiquitination and tubular ER function independently of the host ubiquitin machinery.

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Section: Resultsmentioning

confidence: 99%

A Single Legionella Effector Catalyzes a Multistep Ubiquitination Pathway to Rearrange Tubular Endoplasmic Reticulum for Replication

Kotewicz

Ramabhadran

Sjoblom

et al. 2017

Cell Host & Microbe

181

267

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“…Several of the vertebrate ADPribosyltransferases have the capacity to ADP-ribosylate several eukaryotic target proteins (11,12) and to ADP-ribosylate at two independent sites (13,14), which identified functional relationships with ExoS. Using the tFASTA algorithm, the vertebrate ADP-ribosyltransferases were observed to possess considerable primary amino acid homology with the catalytic portion of ExoS.…”

Section: Identification Of Primary Amino Acid Homology Between the Camentioning

confidence: 99%

“…Several of the vertebrate ADP-ribosyltransferases have the capacity to ADP-ribosylate multiple target proteins. For example, a murine lymphocyte transferase ADP-ribosylates a number of cell surface proteins (11), whereas rabbit skeletal muscle ADP-ribosyltransferase ADP-ribosylates several proteins in skeletal muscle T-tubules (12). In addition, several vertebrate ADP-ribosyltransferases modify target proteins at multiple sites.…”

mentioning

confidence: 99%

Pseudomonas aeruginosa Exoenzyme S, a Double ADP-ribosyltransferase, Resembles Vertebrate Mono-ADP-ribosyltransferases

Ganesan¹,

Mende‐Mueller²,

Selzer³

et al. 1999

Journal of Biological Chemistry

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Previous data indicated thatCystic fibrosis patients, burn wound victims, and the immunocompromised are particularly susceptible to infection by Pseudomonas aeruginosa, a Gram-negative opportunistic pathogen (1). A number of virulence determinants contribute to the pathogenesis of P. aeruginosa, including two ADP-ribosyltransferases, Exotoxin A and Exoenzyme S (ExoS) 1 (2). ExoS is a 49-kDa protein (3) that is secreted by the type III mechanism of P. aeruginosa (4), and ADP-ribosylates a number of target proteins in vitro including apolipoprotein A1, IgG3 (5), vimentin (6), and several members of the Ras superfamily (7). In vivo, ExoS is a cytotoxin (8) that ADP-ribosylates Ras during the course of infection in cultured cells (9), disrupting Ras-mediated signal transduction (10). Indirect methods were used to determine that Exoenzyme S ADP-ribosylates c-Ha-Ras at multiple sites (10).Several vertebrate ADP-ribosyltransferases have been identified to date. The vertebrate ADP-ribosyltransferases possess specific properties that are distinct from the bacterial ADPribosyltransferases. Several of the vertebrate ADP-ribosyltransferases have the capacity to ADP-ribosylate multiple target proteins. For example, a murine lymphocyte transferase ADP-ribosylates a number of cell surface proteins (11), whereas rabbit skeletal muscle ADP-ribosyltransferase ADP-ribosylates several proteins in skeletal muscle T-tubules (12). In addition, several vertebrate ADP-ribosyltransferases modify target proteins at multiple sites. Both turkey erythrocyte type A ADP-ribosyltransferase (13) and chicken ADP-ribosyltransferase (14) ADP-ribosylate actin at two arginine residues. These sites of ADP-ribosylation are located in different regions of actin, which suggests that each ADP-ribosylation event is independent. Although the role of endogenous ADP-ribosylation in the regulation of eukaryotic cell physiology has not been defined in detail, the RT6 transferase appears to be involved in the regulation of T-lymphocyte function (15), and endogenous ADP-ribosylation may contribute to hippocampal long-term potentiation (16).In this study, the ADP-ribosylation of Ras by Exoenzyme S was characterized. Using both mass spectrometry and rpHPLC coupled with Edman degradation, it was determined that ExoS ADP-ribosylates Ras at arginines 41 and 128. These residues are located in a ␤-sheet and ␣-helix, respectively, which are spatially separated in Ras. Thus, ExoS has functional similarities to the eukaryotic ADP-ribosyltransferases because ExoS ADP-ribosylates a number of target proteins in vitro and ADPribosylate Ras at two nonadjacent arginine residues. In addition, homology studies have identified more primary sequence homology between ExoS and the vertebrate ADP-ribosyltransferases than the bacterial ADP-ribosyltransferases.

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“…However, it is important to note that other authors have contested the validity of using biotinylated or digoxigenin-conjugated NAD + as surrogate substrates for ADP-ribosyltransferases. Klebl et al found that the pattern of target proteins labeled by either pertussis toxin or arginine-specific ADP-ribosyltransferase from skeletal muscle was different when using biotinylated or digoxigenin-conjugated NAD + as compared to that obtained using [ 32 P]-NAD + (Klebl et al 1997). …”

Section: Use Of Nonradioactive Nad + Derivativesmentioning

confidence: 99%

Endogenous ADP-Ribosylation

Koch‐Nolte¹

2015

Current Topics in Microbiology and Immunology

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Specificity and Target Proteins of Arginine-Specific Mono-ADP-Ribosylation in T-Tubules of Rabbit Skeletal Muscle

Cited by 7 publications

References 50 publications

A Single Legionella Effector Catalyzes a Multistep Ubiquitination Pathway to Rearrange Tubular Endoplasmic Reticulum for Replication

A Single Legionella Effector Catalyzes a Multistep Ubiquitination Pathway to Rearrange Tubular Endoplasmic Reticulum for Replication

Pseudomonas aeruginosa Exoenzyme S, a Double ADP-ribosyltransferase, Resembles Vertebrate Mono-ADP-ribosyltransferases

Endogenous ADP-Ribosylation

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