F
IPR005502

ADP-ribosylation/Crystallin J1

InterPro entry
Short nameRibosyl_crysJ1
Overlapping
homologous
superfamilies
 
family relationships

Description

This entry represents enzymes that perform ADP-ribosylations, including ADP-ribosylhydrolase ARH1/3 from animals, which preferentially hydrolyses the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine and threonine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose
[4, 7, 3]
.

The family also includes ADP-ribosylarginine hydrolase Tri1 from Serratia proteamaculans. This protein neutralises Tre1-Sp both by occluding its active site via its N-terminal extension and by hydrolysing the ADP-ribosyl moiety from FtsZ. It functions as an immunity component of a contact-dependent interbacterial competition system (also called effector-immunity systems)
[2]
.

ADP-ribosyl-[dinitrogen reductase] glycohydrolase is involved in the regulation of nitrogen fixation activity by the reversible ADP-ribosylation of one subunit of the homodimeric dinitrogenase reductase component of the nitrogenase enzyme complex in Rhodospirillum rubrum
[1, 6]
.

Jellyfish Crystallin proteins
[5]
are also included in this group, although these proteins appear to have lost the presumed active site residues.

References

1.Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum. Fitzmaurice WP, Saari LL, Lowery RG, Ludden PW, Roberts GP. Mol. Gen. Genet. 218, 340-7, (1989). View articlePMID: 2506427

2.Bifunctional Immunity Proteins Protect Bacteria against FtsZ-Targeting ADP-Ribosylating Toxins. Ting SY, Bosch DE, Mangiameli SM, Radey MC, Huang S, Park YJ, Kelly KA, Filip SK, Goo YA, Eng JK, Allaire M, Veesler D, Wiggins PA, Peterson SB, Mougous JD. Cell 175, 1380-1392.e14, (2018). PMID: 30343895

3.Molecular Tools for the Study of ADP-Ribosylation: A Unified and Versatile Method to Synthesise Native Mono-ADP-Ribosylated Peptides. Voorneveld J, Rack JGM, van Gijlswijk L, Meeuwenoord NJ, Liu Q, Overkleeft HS, van der Marel GA, Ahel I, Filippov DV. Chemistry 27, 10621-10627, (2021). PMID: 33769608

4.Hydrolysis of O-acetyl-ADP-ribose isomers by ADP-ribosylhydrolase 3. Kasamatsu A, Nakao M, Smith BC, Comstock LR, Ono T, Kato J, Denu JM, Moss J. J Biol Chem 286, 21110-7, (2011). PMID: 21498885

5.J1-crystallins of the cubomedusan jellyfish lens constitute a novel family encoded in at least three intronless genes. Piatigorsky J, Horwitz J, Norman BL. J. Biol. Chem. 268, 11894-901, (1993). View articlePMID: 8505315

6.Mechanism of ADP-ribosylation removal revealed by the structure and ligand complexes of the dimanganese mono-ADP-ribosylhydrolase DraG. Berthold CL, Wang H, Nordlund S, Hogbom M. Proc. Natl. Acad. Sci. U.S.A. 106, 14247-52, (2009). View articlePMID: 19706507

7.PARP1 inhibition alleviates injury in ARH3-deficient mice and human cells. Mashimo M, Bu X, Aoyama K, Kato J, Ishiwata-Endo H, Stevens LA, Kasamatsu A, Wolfe LA, Toro C, Adams D, Markello T, Gahl WA, Moss J. JCI Insight 4, (2019). PMID: 30830864

Cross References

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