ADP-ribosylation
Oxford Dictionary of Biochemistry:
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ADP-ribosylation
the transfer of one or more adenosinediphosphoribosyl (abbr. ADPribosyl) groups from nicotinamide-adenine dinucleotide, NAD+, to a protein through the action of an ADP-ribosyltransferase. In eukaryotic cells the transfer occurs particularly to the α subunits of G proteins, and then is stimulated by treatment with certain bacterial toxins such as cholera toxin or pertussis toxin. Linear poly(ADPribosyl) attachments, which may consist of up to 50 ADPribose units, are found on nuclear proteins and also on some cytoplasmic proteins. In the stepwise generation of such attachments an incoming ADPribosyl group forms a (12′) glycosidic bond to the nucleosidic ribose moiety of the most recently attached ADPribose unit. ADP-ribosylation occurs also in cells of Escherichia coli infected with bacteriophage T4, where single ADPribosyl groups become attached to the host's RNA polymerase.
—ADP-ribosylated adj. See also ADP-ribosyltransferase, NAD(P)+-arginine ADP-ribosyltransferase.
| ADP-ribosyl cyclase, ADP-Rib, ADP-Glc | |
| ADP-ribosylation factor, ADP-ribosyltransferase, ADPG |
Wikipedia on Answers.com:
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ADP-ribosylation
For other uses, see Par (disambiguation).
ADP-ribosylation is the addition of one or more ADP-ribose moieties to a protein.[1][2] These reactions are involved in cell signaling and the control of many cell processes, including DNA repair and apoptosis.[3][4]
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Contents
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ADP-ribosylation enzymes
One way this protein modification can be produced is by NAD+:diphthamide ADP-ribosyltransferase enzymes, which transfer the ADP-ribose group from nicotinamide adenine dinucleotide (NAD+) onto acceptors such as arginine, glutamic acid, or aspartic acid. In humans, one type of ADP-ribosyltransferases is the NAD:arginine ADP-ribosyltransferases, which modify amino acid residues in proteins such as histones by adding a single ADP-ribose group.[5] These reactions are reversible; for example, when arginine is modified, the ADP-ribosylarginine produced can be removed by ADP-ribosylarginine hydrolases.[6]
Multiple groups of ADP-ribose moieties can also be transferred to proteins to form long branched chains, in a reaction called poly(ADP-ribosyl)ation.[7] This protein modification is carried out by the poly ADP-ribose polymerases (PARPs), which are found in most eukaryotes, but not prokaryotes or yeast.[7][8] The poly(ADP-ribose) structure is involved in the regulation of several cellular events and is most important in the cell nucleus, in processes such as DNA repair and telomere maintenance.[8]
Bacterial toxins
ADP-ribosylation is also responsible for the actions of some bacterial toxins, such as cholera toxin, diphtheria toxin, and pertussis toxin. These toxin proteins are ADP-ribosyltransferases that modify target proteins in human cells. For example, cholera toxin ADP-ribosylates G proteins, causing massive fluid secretion from the lining of the small intestine, resulting in life-threatening diarrhea. P. aeruginosa ADP-ribosylates cytoskeleton and GTP-binding proteins.[9]
See also
References
- ^ Belenky P, Bogan KL, Brenner C (2007). "NAD+ metabolism in health and disease". Trends Biochem. Sci. 32 (1): 12–9. doi:10.1016/j.tibs.2006.11.006. PMID 17161604. http://www.dartmouth.edu/~brenner/belenky07a.pdf.
- ^ Ziegler M (2000). "New functions of a long-known molecule. Emerging roles of NAD in cellular signaling". Eur. J. Biochem. 267 (6): 1550–64. doi:10.1046/j.1432-1327.2000.01187.x. PMID 10712584.
- ^ Berger F, Ramírez-Hernández MH, Ziegler M (2004). "The new life of a centenarian: signalling functions of NAD(P)". Trends Biochem. Sci. 29 (3): 111–8. doi:10.1016/j.tibs.2004.01.007. PMID 15003268.
- ^ Corda D, Di Girolamo M (2003). "NEW EMBO MEMBER'S REVIEW: Functional aspects of protein mono-ADP-ribosylation". EMBO J. 22 (9): 1953–8. doi:10.1093/emboj/cdg209. PMC 156081. PMID 12727863. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=156081.
- ^ Okazaki IJ, Moss J (1999). "Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases". Annual Review of Nutrition 19: 485–509. doi:10.1146/annurev.nutr.19.1.485. PMID 10448534.
- ^ Takada T, Okazaki IJ, Moss J (1994). "ADP-ribosylarginine hydrolases". Mol. Cell. Biochem. 138 (1–2): 119–22. doi:10.1007/BF00928452. PMID 7898453.
- ^ a b Diefenbach J, Bürkle A (2005). "Introduction to poly(ADP-ribose) metabolism". Cell. Mol. Life Sci. 62 (7–8): 721–30. doi:10.1007/s00018-004-4503-3. PMID 15868397.
- ^ a b Burkle A (2005). "Poly(ADP-ribose). The most elaborate metabolite of NAD+". FEBS J. 272 (18): 4576–89. doi:10.1111/j.1742-4658.2005.04864.x. PMID 16156780.
- ^ De Haan L, Hirst TR (2004). "Cholera toxin: a paradigm for multi-functional engagement of cellular mechanisms (Review)". Mol. Membr. Biol. 21 (2): 77–92. doi:10.1080/09687680410001663267. PMID 15204437.
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