Simultaneous determination of linear and branched residues in poly(ADP-ribose)

Juarez-Salinas, Hector; Mendoza-Alvarez, Hilda; Levi, Viktorya; Jacobson, Myron K.; Jacobson, Elaine L.

doi:10.1016/0003-2697(83)90192-6

Cited by 25 publications

(18 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…5 ) ; there was no evidence of the three other 5'-nucleotides and the polymer is not poly(A) because of the presence of (phosphoribosy1)-AMP. The apparent absence of (phosphoribosyl),-AMP indicates that these poly(ADP-ribose) molecules in maize nuclei may contain very few or no branching points (Miwa et al, 1979;Juarez-Salinas et al, 1983).…”

Section: Discussionmentioning

confidence: 99%

Poly(ADP‐Ribose) Polymerase in Plant Nuclei

Chen

Shall

O'Farrell

1994

European Journal of Biochemistry

View full text Add to dashboard Cite

We show that poly(ADP-ribose) polymerase is present in maize, pea and wheat nuclei. We have identified the enzyme product as poly(ADP-ribose) by purification and electrophoresis on a DNA sequencing gel. This reveals a polymer ladder consisting of up to 45 residues. The polymer product from maize, after digestion with snake venom phosphodiesterase, gave only 5'-AMP and (phosphoribosy1)-AMP; the mean chain length of the polymer was 5 and 11 residues in two separate experiments. The optimum pH of the plant enzyme is greater than pH 7.0 in pea, wheat and maize; the optimum temperature for enzyme activity is approximately 15 "C. The K, for NAD' for the enzyme from maize is estimated to be approximately 50 pM under optimal conditions. Several compounds (nicotinamide, deoxythymidine, 3-aminobenzamide, 3-methoxybenzamide and 5-bromodeoxyuridine) that specifically inhibit the animal enzyme also inhibit the enzyme from plants. The ratio of the IC,, for 5-bromodeoxyuridine to the IC,, for 3-aminobenzamide in maize is similar to that of the animal enzyme indicating that the enzyme involved is poly(ADP-ribose) polymerase and not mono(ADP-ribosyl) transferase. SDS gel electrophoresis and gel filtration analysis of a crude extract of maize nuclei indicate a molecular mass for poly(ADP-ribose) polymerase of approximately 114 kDa.

show abstract

Section: Discussionmentioning

confidence: 99%

Poly(ADP‐Ribose) Polymerase in Plant Nuclei

Chen

Shall

O'Farrell

1994

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…The ADP-ribose units in the polymer are linked by glycosidic ribose-ribose 1Ј-2Ј bonds. The chain length of polymers is heterogeneous and can reach 200 to 400 units in vitro and in vivo (16,181,182,186,276). Long polymers are branched in an irregular manner.…”

Section: Poly-adp-ribosylation Cyclementioning

confidence: 99%

“…Long polymers are branched in an irregular manner. Branching occurs in vitro and in vivo with a frequency of approximately one branch per linear section of 20 to 50 units of ADP-ribose (16,181,182,186,276). The chemical structure of the branching site of poly-ADP-ribose was determined by nuclear magnetic resonance and mass spectroscopy (MS) and found to be the same as in the linear regions of the polymer (276).…”

Section: Poly-adp-ribosylation Cyclementioning

confidence: 99%

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Hassa

Haenni

Elser

et al. 2006

Microbiol Mol Biol Rev

631

644

View full text Add to dashboard Cite

SUMMARY Since poly-ADP ribose was discovered over 40 years ago, there has been significant progress in research into the biology of mono- and poly-ADP-ribosylation reactions. During the last decade, it became clear that ADP-ribosylation reactions play important roles in a wide range of physiological and pathophysiological processes, including inter- and intracellular signaling, transcriptional regulation, DNA repair pathways and maintenance of genomic stability, telomere dynamics, cell differentiation and proliferation, and necrosis and apoptosis. ADP-ribosylation reactions are phylogenetically ancient and can be classified into four major groups: mono-ADP-ribosylation, poly-ADP-ribosylation, ADP-ribose cyclization, and formation of O-acetyl-ADP-ribose. In the human genome, more than 30 different genes coding for enzymes associated with distinct ADP-ribosylation activities have been identified. This review highlights the recent advances in the rapidly growing field of nuclear mono-ADP-ribosylation and poly-ADP-ribosylation reactions and the distinct ADP-ribosylating enzyme families involved in these processes, including the proposed family of novel poly-ADP-ribose polymerase-like mono-ADP-ribose transferases and the potential mono-ADP-ribosylation activities of the sirtuin family of NAD+-dependent histone deacetylases. A special focus is placed on the known roles of distinct mono- and poly-ADP-ribosylation reactions in physiological processes, such as mitosis, cellular differentiation and proliferation, telomere dynamics, and aging, as well as “programmed necrosis” (i.e., high-mobility-group protein B1 release) and apoptosis (i.e., apoptosis-inducing factor shuttling). The proposed molecular mechanisms involved in these processes, such as signaling, chromatin modification (i.e., “histone code”), and remodeling of chromatin structure (i.e., DNA damage response, transcriptional regulation, and insulator function), are described. A potential cross talk between nuclear ADP-ribosylation processes and other NAD+-dependent pathways is discussed.

show abstract

“…Although the molecular mechanism of inhibition of DNAS1L3 by PARP-1 is not well established, the attachment of long, branched chains of ADP-ribose (38,39) to the endonuclease by PARP-1 likely results in a marked decrease in its binding affinity for DNA (14). Such a reduction in binding affinity probably results from repulsion between the negative charges associated with both PAR and DNA.…”

mentioning

confidence: 99%

Regulation of DNAS1L3 Endonuclease Activity by Poly(ADP-ribosyl)ation during Etoposide-induced Apoptosis

Boulares¹,

Zoltoski²,

Contreras³

et al. 2002

Journal of Biological Chemistry

View full text Add to dashboard Cite

Apoptosis plays important roles in immunity, development, and homeostasis as well as in the response to cell injury. This process of programmed cell death is characterized by marked changes in cell morphology, including chromatin condensation, membrane blebbing, nuclear breakdown, and the appearance of membrane-associated apoptotic bodies, as well as by internucleosomal DNA fragmentation and the cleavage of many housekeeping proteins such as poly(ADP-ribose) polymerase-1 (PARP-1) 1 and lamins. Apoptosis is triggered by various agents, including endogenous cytokines as well as therapeutic and cytotoxic drugs, and its initiation and execution are mediated by activation of members of the caspase family of aspartate-specific cysteine proteases.

show abstract

Simultaneous determination of linear and branched residues in poly(ADP-ribose)

Cited by 25 publications

References 32 publications

Poly(ADP‐Ribose) Polymerase in Plant Nuclei

Poly(ADP‐Ribose) Polymerase in Plant Nuclei

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Regulation of DNAS1L3 Endonuclease Activity by Poly(ADP-ribosyl)ation during Etoposide-induced Apoptosis

Contact Info

Product

Resources

About