ADP ribosylation of rat liver nucleosomal core histones.

Burzio, Luis O.; Riquelme, Patricio T.; Koide, S. S.

doi:10.1016/s0021-9258(17)30178-3

Cited by 185 publications

(36 citation statements)

References 39 publications

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“…Nuclear proteins, such as core histones, were identified as substrates for ADPRylation decades ago (Burzio et al, 1979;Hilz and Stone, 1976;Jump et al, 1979;Minaga et al, 1979). However, unlike other well-characterized histone modifications (e.g., acetylation, methylation, and phosphorylation) (Lawrence et al, 2016), the sites of histone ADPRylation are poorly characterized, and the functions of histone ADPRylation are unknown.…”

Section: Introductionmentioning

confidence: 99%

Functional Interplay between Histone H2B ADP-Ribosylation and Phosphorylation Controls Adipogenesis

et al. 2020

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Section: Introductionmentioning

confidence: 99%

Functional Interplay between Histone H2B ADP-Ribosylation and Phosphorylation Controls Adipogenesis

et al. 2020

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“…It needs to be noted that even after 4 h of exposure to neutral hydroxylamine, a residual signal is still present. The halftime of the MARylation on glutamates is around 10 min in neutral hydroxylamine and with longer incubation times also arginine modification will be lost [ 56–58 ]. This experiment can thus not differentiate between glutamate and arginine modification, especially considering that the shortest time-point analysed here was 1 h [ 4 ].…”

Section: Parp10mentioning

confidence: 99%

“…As briefly mentioned above, it was thought previously that PARPs modify acidic or basic residues [ 2 , 4 , 56 , 81–83 ], which has been challenged by different specificities of PARP1/HPF1 [ 23 ], PARP7 [ 24 , 25 , 80 ] and PARP10 [ 59 , 60 ]. Investigating all PARP enzymes using traditional biochemical methods such as chemical and hydrolase treatments may be highly time-consuming and error-prone, as it again relies on high amounts of recombinant enzyme analysed in artificial settings.…”

Section: Chemical Genetics and Mass-spectrometry Based Studies To Ide...mentioning

confidence: 99%

Are PARPs promiscuous?

Feijs

Žaja

2022

Bioscience Reports

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Posttranslational modifications exist in different varieties to regulate diverse characteristics of their substrates, ultimately leading to maintenance of cell health. The enzymes of the intracellular PARP family can transfer either a single ADP-ribose to targets, in a reaction called mono(ADP-ribosyl)ation or MARylation, or multiple to form chains of poly(ADP-ribose) or PAR. Traditionally thought to be attached to arginine or glutamate, recent data have added serine, tyrosine, histidine and others to the list of potential ADP-ribose acceptor amino acids. PARylation by PARP1 has been relatively well studied, whereas less is known about the other family members such as PARP7 and PARP10. ADP-ribosylation on arginine and serine is reversed by ARH1 and ARH3 respectively, whereas macrodomain-containing MACROD1, MACROD2 and TARG1 reverse modification of acidic residues. For the other amino acids, no hydrolases have been identified to date. For many PARPs, it is not clear yet what their endogenous targets are. Better understanding of their biochemical reactions is required to be able to determine their biological functions in future studies. In this review, we discuss the current knowledge of PARP specificity in vitro and in cells, as well as provide an outlook for future research.

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“…A few glutamate residues in H1 and H2B histones are the preferred acceptor sites for poly-ADP-ribosylation in native chromatin [143,144]. None of them, however, have been ultimately confirmed by mass spectrometry, probably due to the extremely reduced fraction of ADP-ribosylated histones, which is less than 1% of the total amount [145,146].…”

Section: Adp-ribosylationmentioning

confidence: 99%

The Expanding Constellation of Histone Post-Translational Modifications in the Epigenetic Landscape

Cavalieri

2021

Genes

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The emergence of a nucleosome-based chromatin structure accompanied the evolutionary transition from prokaryotes to eukaryotes. In this scenario, histones became the heart of the complex and precisely timed coordination between chromatin architecture and functions during adaptive responses to environmental influence by means of epigenetic mechanisms. Notably, such an epigenetic machinery involves an overwhelming number of post-translational modifications at multiple residues of core and linker histones. This review aims to comprehensively describe old and recent evidence in this exciting field of research. In particular, histone post-translational modification establishing/removal mechanisms, their genomic locations and implication in nucleosome dynamics and chromatin-based processes, as well as their harmonious combination and interdependence will be discussed.

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ADP ribosylation of rat liver nucleosomal core histones.

Cited by 185 publications

References 39 publications

Functional Interplay between Histone H2B ADP-Ribosylation and Phosphorylation Controls Adipogenesis

Functional Interplay between Histone H2B ADP-Ribosylation and Phosphorylation Controls Adipogenesis

Are PARPs promiscuous?

The Expanding Constellation of Histone Post-Translational Modifications in the Epigenetic Landscape

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