Table 1.

A Biological Toolbox of ADP-Ribose Binding and Hydrolysis Protein Domains

Our current understanding of the most well-studied ADP-ribose binding domains and hydrolases. Green = Yes, Red = No, E/R = hydrolysis shown specifically for glutamate or arginine residues, respectively. MD = macrodomain, N/A = not applicable, blank = possible but currently unknown. SARS-CoV, Severe Acute Respiratory Syndrome-Coronavirus; HEV, Hepatitis E Virus; SFV, Semliki Forest Virus.

^aJankevicius et al., 2013, Rosenthal et al., 2013, Timinszky et al., 2009

^bAhel et al., 2009, Gottschalk et al., 2012, Karras et al., 2005

^cEgloff et al., 2006, Neuvonen and Ahola, 2009

^dDaniels et al., 2014, Jankevicius et al., 2013, Karras et al., 2005, Rosenthal et al., 2013

^e,fJankevicius et al., 2013, Neuvonen and Ahola, 2009, Rosenthal et al., 2013

^gmouse PARP-14 macrodomain 2; Forst et al., 2013, Rosenthal et al., 2013

^hAhel et al., 2008, Oberoi et al., 2010

ⁱHe et al., 2012, Wang et al., 2012

^jEgloff et al., 2006, Neuvonen and Ahola, 2009

^kGagné et al., 2012, Rosenthal et al., 2013, Slade et al., 2011

^lTARG1 removes the complete PAR chain from modified glutamate residues, rather than hydrolyzing glycosidic bonds between subunits of PAR as in PARG and ARH3; Rosenthal et al., 2013, Sharifi et al., 2013

^mKonczalik and Moss, 1999, Ohno et al., 1995, Oka et al., 2006

ⁿMueller-Dieckmann et al., 2006, Oka et al., 2006, Rosenthal et al., 2011

^∗ARH3 showed no hydrolase activities against MARylated arginine, cysteine, diphthamide, and asparagine