Amino acid-specific ADP-ribosylation. Sensitivity to hydroxylamine of [cysteine(ADP-ribose)]protein and [arginine(ADP-ribose)]protein linkages.

Hsia, Judith; Tsai, Su-Chen; Adamik, Ronald; Yost, David A.; Hewlett, Erik L.; Moss, Joel

doi:10.1016/s0021-9258(17)36219-1

Cited by 74 publications

(16 citation statements)

References 32 publications

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“…Hydroxylamine resistance of labeling (Fig. S2 A, seventh lane) suggests modification of Arg or Cys residues rather than glutamate, as the latter forms a labile carboxylate ester bond to the ADP-ribose moiety (Hsia et al, 1985).…”

Section: Adp Ribosylation-mimetic Charge Substitutions Destabilize Substrate Binding By Bipmentioning

confidence: 99%

ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load

Chambers

Petrova

Tomba

et al. 2012

Journal of Cell Biology

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Section: Adp Ribosylation-mimetic Charge Substitutions Destabilize Substrate Binding By Bipmentioning

confidence: 99%

ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load

Chambers

Petrova

Tomba

et al. 2012

Journal of Cell Biology

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“…We next sought to identify the amino acid ADPr acceptors in PARP-13 that are MARylated by PARP-7 using chemical stability studies. NH 2 OH cleaves the ester bond between Glu/Asp and ADPr whereas HgCl 2 cleaves the thioether bond between Cys and ADPr (Figure 4a) 9 . We co-expressed HA-PARP-13.2 with either GFP-PARP-7 or GFP-PARP-10 in HEK 293T cells and evaluated MARylation by Western blot analysis using an ADPr-specific antibody.…”

Section: Cys Residues Are the Major Sites Of Parp-7-mediated Marylation In Parp-13mentioning

confidence: 99%

“…A unique feature of MARylation compared to other PTMs is that chemically diverse amino acids can act as ADP-ribose (ADPr) acceptors 6 . Historically, the chemical nature of the amino acid-MAR bonds in proteins was examined by chemical stability studies 7,8,9,10,11 . This led to the notion that the major ADPr acceptor residues are the acidic amino acids, glutamate (Glu) and aspartate (Asp), as well as the basic amino acid arginine (Arg).…”

Section: Introductionmentioning

confidence: 99%

Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets

Rodriguez

Buch-Larsen

Kirby

et al. 2021

eLife

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Poly(ADP-ribose) polymerase 7 (PARP-7) has emerged as a critically important member of a large enzyme family that catalyzes ADP-ribosylation in mammalian cells. PARP-7 is a critical regulator of the innate immune response. What remains unclear is the mechanism by which PARP-7 regulates this process, namely because the protein targets of PARP-7 mono-ADP-ribosylation (MARylation) are largely unknown. Here, we combine chemical genetics, proximity labeling, and proteome-wide amino acid ADP-ribosylation site profiling for identifying the direct targets and sites of PARP-7-mediated MARylation in a cellular context. We found that the inactive PARP family member, PARP-13—a critical regulator of the antiviral innate immune response—is a major target of PARP-7. PARP-13 is preferentially MARylated on cysteine residues in its RNA binding zinc finger domain. Proteome-wide ADP-ribosylation analysis reveals cysteine as a major MARylation acceptor of PARP-7. This study provides insight into PARP-7 targeting and MARylation site preference.

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“…that modify over 30 host proteins: Alt is injected into the bacterium together with the phage DNA and immediately ADP-ribosylates E. coli RNAP at different positions, thought to result in the preferential transcription of phage genes from "early" promoters 17,18 . Two early phage genes code for the ARTs ModA 19 and ModB 2,20 . The former completes ADP-ribosylation of RNAP, while the latter modifies a set of host proteins mostly involved in translation 18 .…”

mentioning

confidence: 99%

A viral ADP-ribosyltransferase attaches RNA chains to host proteins

Höfer

Wolfram-Schauerte

Grawenhoff

et al. 2021

Preprint

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The mechanisms by which viruses hijack their host's genetic machinery are of enormous current interest. One mechanism is adenosine diphosphate (ADP) ribosylation, where ADP-ribosyltransferases (ARTs) transfer an ADP-ribose fragment from the ubiquitous coenzyme nicotinamide adenine dinucleotide (NAD) to acceptor proteins. When bacteriophage T4 infects Escherichia coli, three different ARTs reprogram the host's transcriptional and translational apparatus. Recently, NAD was identified as a 5'-modification of cellular RNA molecules in bacteria and higher organisms. Here, we report that bacteriophage T4 ARTs accept not only NAD, but also NAD-RNA as substrate, thereby covalently linking entire RNA chains to acceptor proteins in an "RNAylation" reaction. One of these ARTs, ModB, efficiently RNAylates its host protein target, ribosomal protein S1, at arginine residues and strongly prefers NAD-RNA over NAD. Mutation of a single arginine at position 139 abolishes ADP-ribosylation and RNAylation. Overexpression of mammalian ADP-ribosylarginine hydrolase 1 (ARH1), which cleaves arginine-phosphoribose bonds, shows a decelerated lysis of E. coli when infected with T4. Our findings not only challenge the established views of the phage replication cycle, but also reveal a distinct biological role of NAD-RNA, namely activation of the RNA for enzymatic transfer. Our work exemplifies the first direct connection between RNA modification and post-translational protein modification. As ARTs play important roles in different viral infections, as well as in antiviral defence by the host, RNAylation may have far-reaching implications.

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Amino acid-specific ADP-ribosylation. Sensitivity to hydroxylamine of [cysteine(ADP-ribose)]protein and [arginine(ADP-ribose)]protein linkages.

Cited by 74 publications

References 32 publications

ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load

ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load

Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets

A viral ADP-ribosyltransferase attaches RNA chains to host proteins

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