ADP-ribosylation: Difference between revisions

From Wikipedia, the free encyclopedia
Browse history interactively
← Previous editNext edit →
Content deleted Content added
VisualWikitext
reword
Line 1: Line 1:
[[Image:Adenosine diphosphate ribose.svg|thumb|250px|[[Adenosine diphosphate ribose|ADP ribose]]]]
[[Image:Adenosine diphosphate ribose.svg|thumb|250px|[[Adenosine diphosphate ribose|ADP ribose]]]]
'''ADP-ribosylation''' is a [[posttranslational modification]] that involves the addition of an [[ADP]] and [[ribose]] moiety onto the target protein.<ref>{{cite journal |author=Belenky P, Bogan KL, Brenner C |title=NAD+ metabolism in health and disease |journal=Trends Biochem. Sci. |volume=32 |issue=1 |pages=12-9 |year=2007 |pmid=17161604 |url=http://www.dartmouth.edu/~brenner/belenky07a.pdf}}</ref><ref>{{cite journal |author=Ziegler M |title=New functions of a long-known molecule. Emerging roles of NAD in cellular signaling |journal=Eur. J. Biochem. |volume=267 |issue=6 |pages=1550-64 |year=2000 |pmid=10712584}}</ref> These reactions are involved in [[cell signaling]] and the control of many cell processes, including [[DNA repair]] and [[apoptosis]].<ref>{{cite journal |author=Berger F, Ramírez-Hernández MH, Ziegler M |title=The new life of a centenarian: signalling functions of NAD(P) |journal=Trends Biochem. Sci. |volume=29 |issue=3 |pages=111-8 |year=2004 |pmid=15003268}}</ref>
'''ADP-ribosylation''' is a [[posttranslational modification]] of [[protein]]s that involves the addition of one or more [[ADP]] and [[ribose]] moieties.<ref>{{cite journal |author=Belenky P, Bogan KL, Brenner C |title=NAD+ metabolism in health and disease |journal=Trends Biochem. Sci. |volume=32 |issue=1 |pages=12-9 |year=2007 |pmid=17161604 |url=http://www.dartmouth.edu/~brenner/belenky07a.pdf}}</ref><ref>{{cite journal |author=Ziegler M |title=New functions of a long-known molecule. Emerging roles of NAD in cellular signaling |journal=Eur. J. Biochem. |volume=267 |issue=6 |pages=1550-64 |year=2000 |pmid=10712584}}</ref> These reactions are involved in [[cell signaling]] and the control of many cell processes, including [[DNA repair]] and [[apoptosis]].<ref>{{cite journal |author=Berger F, Ramírez-Hernández MH, Ziegler M |title=The new life of a centenarian: signalling functions of NAD(P) |journal=Trends Biochem. Sci. |volume=29 |issue=3 |pages=111-8 |year=2004 |pmid=15003268}}</ref>


==ADP-ribosylation enzymes==
==ADP-ribosylation enzymes==

Revision as of 16:36, 12 September 2007

ADP ribose

ADP-ribosylation is a posttranslational modification of proteins that involves the addition of one or more ADP and ribose moieties.[1][2] These reactions are involved in cell signaling and the control of many cell processes, including DNA repair and apoptosis.[3]

ADP-ribosylation enzymes

This protein modification is produced by ADP-ribosyltransferase enzymes, which transfer the ADP-ribose group from nicotinamide adenine dinucleotide (NAD+) onto acceptors such as arginine, glutamic acid or aspartic acid residues in their substrate protein. In humans, the best-understood type of ADP-ribosyltransferases are the NAD:arginine ADP-ribosyltransferases, which modify proteins such as histones.[4] The ADP-ribosylarginine modification produced by these enzymes is removed from proteins by ADP-ribosylarginine hydrolases.[5]

ADP-ribose can also be transferred to proteins in long branched chains, in a reaction called poly(ADP-ribosyl)ation.[6] This protein modification is carried out by the poly ADP-ribose polymerases (PARPs) which are found in most eukaryotes, but not prokaryotes or yeast.[6][7] The poly(ADP-ribose) structure is involved in the regulation of several cellular processes and is most important in nuclear functions, such as DNA repair and telomere maintenance.[7]

Bacterial toxins

ADP-ribosylation is also responsible for the actions of several bacterial toxins, such as cholera 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, which causes massive fluid secretion from the lining of the small intestine and results in life-threatening diarrhea.[8]

See also

References

  1. ^ Belenky P, Bogan KL, Brenner C (2007). "NAD+ metabolism in health and disease" (PDF). Trends Biochem. Sci. 32 (1): 12–9. PMID 17161604.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ Ziegler M (2000). "New functions of a long-known molecule. Emerging roles of NAD in cellular signaling". Eur. J. Biochem. 267 (6): 1550–64. PMID 10712584.
  3. ^ 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. PMID 15003268.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  4. ^ Okazaki IJ, Moss J (1999). "Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases". Annu. Rev. Nutr. 19: 485–509. PMID 10448534.
  5. ^ Takada T, Okazaki IJ, Moss J (1994). "ADP-ribosylarginine hydrolases". Mol. Cell. Biochem. 138 (1–2): 119–22. PMID 7898453.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  6. ^ a b Diefenbach J, Bürkle A (2005). "Introduction to poly(ADP-ribose) metabolism". Cell. Mol. Life Sci. 62 (7–8): 721–30. PMID 15868397.
  7. ^ a b Burkle A (2005). "Poly(ADP-ribose). The most elaborate metabolite of NAD+". FEBS J. 272 (18): 4576–89. PMID 16156780.
  8. ^ 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. PMID 15204437.


Stub icon

This biochemistry article is a stub. You can help Wikipedia by expanding it.

Retrieved from "https://en.wikipedia.org/w/index.php?title=ADP-ribosylation&oldid=157408536"