Biosynthesis and Degradation of Poly(ADP-Ribose) Synthetase

Kameshita, Isamu; Mitsuuchi, Yasuhiro; Matsuda, Michiko; Shizuta, Yutaka

doi:10.1007/978-1-4615-8507-7_13

Cited by 19 publications

(28 citation statements)

References 11 publications

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“…This apparent selectivity is unexplained, unless one considers macromolecular structural factors such as dimerization [18] that may determine this selectivity towards DEP under given experimental conditions. Our results thus provide preliminary evidence for the localization of the catalytic site of ADPRT in the 56 kDa carboxy-terminal polypeptide domain, coinciding with a previous suggestion [19], which is based on specific thiol labelling of ADPT. The participation of both SH and histidyl residues in the formation of an unstable ADPR-histidyl adduct appears reasonable and provides the first indication of the chemical nature of the previously observed highly base unstable mono ADPR adduct [7].…”

Section: Discussionsupporting

confidence: 91%

Evidence for the participation of histidine residues located in the 56 kDa C‐terminal polypeptide domain of ADP‐ribosyl transferase in its catalytic activity

1990

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Purified ADPRT protein was inactivated by the histidine specific reagent diethylpyrocarbonate, binding to two histidine residues, or by a relatively histidine selective photoinactivation method. Inactivation with up to 1.3 mM diethylpyrocarbonate was reversible by hydroxylamine. Enzymatic inactivation coincided with the loss of binding capacity of the enzyme protein to benzamide affinity matrix but not to DNA cellulose. Labelled diethylpyrocarbonate was identified exclusively in the 56 kDa carboxyl-terminal polypeptide where 2 out of 13 histidine residues were modified by this reagent. It is proposed that histidine residues in the 56 kDa polypeptide may participate as initiator sites for polyADP-ribosylation.

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Section: Discussionsupporting

confidence: 91%

Evidence for the participation of histidine residues located in the 56 kDa C‐terminal polypeptide domain of ADP‐ribosyl transferase in its catalytic activity

1990

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“…1 and 2). It is made up of three functional domains, namely the amino-terminal DNA-binding domain, the central automodification domain, and the carboxyl-terminal catalytic domain (3). Although PARP-1 is often associated with DNA repair, because of its rapid and extensive activation following DNA damage (4,5), it has also been implicated in other major nuclear functions such as transcription (6,7), DNA replication (8,9) and recombination (10).…”

mentioning

confidence: 99%

Nuclear Factor 1 Interferes with Sp1 Binding through a Composite Element on the Rat Poly(ADP-ribose) Polymerase Promoter to Modulate Its Activity in Vitro

Laniel

Poirier

Guérin

2001

Journal of Biological Chemistry

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Poly(ADP-ribose) polymerase-1 (PARP-1) catalyzes the rapid and extensive poly(ADP-ribosyl)ation of nuclear proteins in response to DNA strand breaks, and its expression, although ubiquitous, is modulated from tissue to tissue and during cellular differentiation. PARP-1 gene promoters from human, rat, and mouse have been cloned, and they share a structure common to housekeeping genes, as they lack a functional TATA box and contain multiple GC boxes, which bind the transcriptional activator Sp1. We have previously shown that, although Sp1 is important for rat PARP1 (rPARP) promoter activity, its finely tuned modulation is likely dependent on other transcription factors that bind the rPARP proximal promoter in vitro. In this study, we identified one such factor as NF1-L, a rat liver isoform of the nuclear factor 1 family of transcription factors. The NF1-L site on the rPARP promoter overlaps one of the Sp1 binding sites previously identified, and we demonstrated that binding of both factors to this composite element is mutually exclusive. Furthermore, we provide evidence that NF1-L has no effect by itself on rPARP promoter activity, but rather down-regulates the Sp1 activity by interfering with its ability to bind the rPARP promoter in order to modulate transcription of the rPARP gene.Poly(ADP-ribose) polymerase-1 (PARP-1) 1 is a nuclear enzyme which catalyzes the addition of ADP-ribose units from nicotinamide adenine dinucleotide (NAD ϩ ) onto itself and other nuclear proteins such as histones and topoisomerases (reviewed in Refs. 1 and 2). It is made up of three functional domains, namely the amino-terminal DNA-binding domain, the central automodification domain, and the carboxyl-terminal catalytic domain (3). Although PARP-1 is often associated with DNA repair, because of its rapid and extensive activation following DNA damage (4, 5), it has also been implicated in other major nuclear functions such as transcription (6, 7), DNA replication (8, 9) and recombination (10). PARP-1 is also important for cell differentiation (11-13) and is involved in cell death, likely acting as a molecular switch between apoptosis and necrosis (14).PARP-1 is expressed in all organs, albeit at varying degrees, with highest mRNA expression found in brain, thymus, heart, and testis (15, 16). PARP-1 mRNA level is regulated at the cell cycle level, reaching its peak at either the G 1 (17-20) or the S phases (21, 22). It has also been shown that a decrease in PARP-1 mRNA levels is associated with cellular differentiation (23-26) and senescence (27), whereas an increase is observed upon activation of lymphocytes (17, 28) or peripheral blood mononuclear cells (18). All these studies show that, although PARP-1 is ubiquitously expressed, its modulation, likely through complex transcriptional regulation, is critical to major cellular functions.In order to better understand the transcriptional mechanisms regulating PARP-1 expression, the PARP-1 gene promoter has been identified and cloned from three mammalian species, human (29, 30), rat (31), ...

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“…Since the human [lo] and rat [7] sequences are homologous around the catalytic domain putative internal start site (not shown) described before [lo], we feel that this 40 kDa fragment more likely derives from the cleavage of the human domain by an endogenous a-chymotrypsinlike protease of E. co/i. a-Chymotrypsin was previously shown to cut in the human [17] and bovine [2,4,18] 55 kDa catalytic domain to generate 40 and 15 kDa fragments. We thus compared the predicted amino acid sequence of the PARP from different organisms at this cleavage site (Fig.…”

Section: Resultsmentioning

confidence: 99%

Expression in E.coli of the catalytic domain of rat poly(ADP‐ribose)polymerase

Thibodeau¹,

Simonin²,

Favazza³

et al. 1990

FEBS Letters

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A 2 kilobase pair cDNA coding for the entire C-terminal catalytic domain of rat poly(ADP-riiose)polymerase has been expressed in E. coli. The overproduced 55 kDa polypeptide is active in synthesizing poly(ADP-ribose) and the 4 kDa N-terminal region of this domain is recognized by the monoclonal antibody C I,2 directed against the calf enzyme. Also, the minor a-chymotrypsin cleavage site found in the human catalytic domain is not present in the rat enzyme as revealed by the absence of the 40 kDa specific degradation product in the E. coli cells expressing the rat domain. The expression of this partial rat cDNA should thus permit the rapid purification and subsequent crystallization of the catalytic domain of the enzyme.

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Biosynthesis and Degradation of Poly(ADP-Ribose) Synthetase

Cited by 19 publications

References 11 publications

Evidence for the participation of histidine residues located in the 56 kDa C‐terminal polypeptide domain of ADP‐ribosyl transferase in its catalytic activity

Evidence for the participation of histidine residues located in the 56 kDa C‐terminal polypeptide domain of ADP‐ribosyl transferase in its catalytic activity

Nuclear Factor 1 Interferes with Sp1 Binding through a Composite Element on the Rat Poly(ADP-ribose) Polymerase Promoter to Modulate Its Activity in Vitro

Expression in E.coli of the catalytic domain of rat poly(ADP‐ribose)polymerase

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