Regulation of <i>S</i>-adenosylmethionine decarboxylase activity by alterations in the intracellular polyamine content

Shantz, Lisa M.; Holm, Ingvar; Jänne, Olli A.; Pegg, Anthony E.

doi:10.1042/bj2880511

Cited by 58 publications

(68 citation statements)

References 37 publications

(41 reference statements)

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“…The PEST sequence has been reported to be located in some proteins with fast turnover rates and be essential for the interaction between SCF complex and target proteins, which consequently leads to ubiquitination/26S proteasome-mediated degradation (Kiernan et al, 2001;Berset et al, 2002;Blondel et al, 2005;Pal et al, 2007). Human SAMDC was reported to have a short half-life and is regulated at multiple levels, such as the transcriptional, translational, and posttranslational levels (Shantz et al, 1992;Stanley et al, 1994;Hanfrey et al, 2003;Yerlikaya and Stanley, 2004). Taking all the information above together, we wanted to ask whether the interaction with BSCTV C2 can affect with the stability of SAMDC1.…”

Section: Bsctv C2 Interacts With Arabidopsis Samdc1mentioning

confidence: 99%

“…Our results of the wheat germ and Arabidopsis cell-free assays also indicated that Arabidopsis SAMDC1 is degraded in a similar 26S proteasome-dependent manner. Cellular activity of SAMDC is reported to be regulated at multiple levels, such as transcriptional, translational, and posttranslational (Shirahata and Pegg, 1986;Kameji and Pegg, 1987;Pegg, 1988;Pegg et al, 1988;Stanley et al, 1989;Shantz et al, 1992), one of which is likely mediated by a cellular protein degradation system. Our wheat germ and Arabidopsis cell-free assay data suggested that BSCTV C2 may positively regulate SAMDC1 at a posttranslational level.…”

Section: Bsctv C2 Positively Regulates Samdc1mentioning

confidence: 99%

“…SAMDCs in many organisms are highly conserved, sharing a defined autocleavage recognition site and a PEST region enriched in Pro (P), Glu (E), Ser (S), and Thr (T) that is correlated with the protein's rapid turnover (Salama et al, 1994;Rechsteiner and Rogers, 1996;Berset et al, 2002;Blondel et al, 2005;Pal et al, 2007). SAMDC is expressed throughout the cell, and its expression is regulated at multiple levels, such as the transcriptional, translational, and posttranslational levels (Shantz et al, 1992;Stanley et al, 1994;Hanfrey et al, 2003;Yerlikaya and Stanley, 2004). Previous studies indicated that SAMDC is involved in diverse growth and developmental processes, including cell division, cell proliferation and differentiation, morphological development, and response to abiotic stress (Kumar et al, 1996;Frostesjö et al, 1997;Shibata et al, 1998;Wi et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

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BSCTV C2 Attenuates the Degradation of SAMDC1 to Suppress DNA Methylation-Mediated Gene Silencing in Arabidopsis

et al. 2011

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Plant viruses are excellent tools for studying microbial-plant interactions as well as the complexities of host activities. Our study focuses on the role of C2 encoded by Beet severe curly top virus (BSCTV) in the virus-plant interaction. Using BSCTV C2 as bait in a yeast two-hybrid screen, a C2-interacting protein, S-adenosyl-methionine decarboxylase 1 (SAMDC1), was identified from an Arabidopsis thaliana cDNA library. The interaction was confirmed by an in vitro pull-down assay and a firefly luciferase complemention imaging assay in planta. Biochemical analysis further showed that the degradation of the SAMDC1 protein was inhibited by MG132, a 26S proteasome inhibitor, and that C2 could attenuate the degradation of the SAMDC1 protein. Genetic analysis showed that loss of function of SAMDC1 resulted in reduced susceptibility to BSCTV infection and reduced viral DNA accumulation, similar to the effect of BSCTV C2 deficiency. Bisulfite sequencing analysis further showed that C2 deficiency caused enhanced DNA methylation of the viral genome in infected plants. We also showed that C2 can suppress de novo methylation in the FWA transgenic assay in the C2 transgene background. Overexpression of SAMDC1 can mimic the suppressive activity of C2 against green fluorescent protein-directed silencing. These results suggest that C2 interferes with the host defense mechanism of DNA methylation-mediated gene silencing by attenuating the 26S proteasome-mediated degradation of SAMDC1.

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Section: Bsctv C2 Interacts With Arabidopsis Samdc1mentioning

confidence: 99%

Section: Bsctv C2 Positively Regulates Samdc1mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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BSCTV C2 Attenuates the Degradation of SAMDC1 to Suppress DNA Methylation-Mediated Gene Silencing in Arabidopsis

et al. 2011

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“…The mature catalytically active enzyme consists of a dimer (␣ 2 ␤ 2 ) of these subunits (5). Cellular AdoMetDC activity is tightly regulated at multiple levels: transcription of the AdoMetDC gene is repressed by spermidine, the translation of its mRNA is negatively regulated by spermine (6), and the processing of the proenzyme and the catalytic activity of the final enzyme are stimulated by the spermidine precursor putrescine (7,8). It has been reported that the half-life of AdoMetDC is inversely related to the cellular content of spermidine and spermine (9 -11), so that when the levels of polyamines are high, increased degradation of AdoMetDC serves as another important control mechanism in maintaining AdoMetDC activity and therefore polyamine levels (3,5).…”

mentioning

confidence: 99%

S-Adenosylmethionine Decarboxylase Degradation by the 26 S Proteasome Is Accelerated by Substrate-mediated Transamination

Yerlikaya

Stanley

2004

Journal of Biological Chemistry

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The short-lived enzyme S-adenosylmethionine decarboxylase uses a covalently bound pyruvoyl cofactor to catalyze the formation of decarboxylated S-adenosylmethionine, which then donates an aminopropyl group for polyamine biosynthesis. Here we demonstrate that S-adenosylmethionine decarboxylase is ubiquitinated and degraded by the 26 S proteasome in vivo, a process that is accelerated by inactivation of S-adenosylmethionine decarboxylase by substrate-mediated transamination of its pyruvoyl cofactor. Proteasome inhibition in COS-7 cells prevents the degradation of S-adenosylmethionine decarboxylase antigen; however, even brief inhibition of the 26 S proteasome caused substantial losses of S-adenosylmethionine decarboxylase activity despite accumulation of S-adenosylmethionine decarboxylase antigen. Levels of the enzyme's substrate (S-adenosylmethionine) increased rapidly after 26 S proteasome inhibition, and this increase in substrate level is consistent with the observed loss of activity arising from an increased rate of inactivation by substrate-mediated transamination. Evidence is also presented that this substrate-mediated transamination accelerates normal degradation of S-adenosylmethionine decarboxylase, as the rate of degradation of the enzyme was increased in the presence of AbeAdo (5 -([(Z)-4-amino-2-butenyl]methylamino]-5 -deoxyadenosine) (a substrate analogue that transaminates the enzyme); conversely, when the intracellular substrate level was reduced by methionine deprivation, the rate of degradation of the enzyme was decreased. Ubiquitination of S-adenosylmethionine decarboxylase is demonstrated by isolation of His-tagged AdoMetDC (S-adenosylmethionine decarboxylase) from COS-7 cells co-transfected with hemagglutinin-tagged ubiquitin and showing bands that were immunoreactive to both anti-AdoMetDC antibody and anti-hemagglutinin antibody. This is the first study to demonstrate that AdoMetDC is ubiquitinated and degraded by the 26 S proteasome, and substrate-mediated acceleration of degradation is a unique finding.

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“…4). ODC activities, or due to a deficit in the activities for spermine synthesis, the intracellular concentrations of dcSAM increase (Frostesjo et al, 1997;Pegg et al, 2011;Shantz et al, 1992;Yamamoto et al, 2010). Simultaneously, such cells have been reported to have enhanced demethylation status of the entire genome (Papazafiri & Osborne, 1987;Tsuji et al, 2001).…”

Section: The Relationship Between Polyamines and Gene Methylationmentioning

confidence: 99%

Biological Effects of Polyamines on the Prevention of Aging-associated Diseases and on Lifespan Extension

Soda

2015

FSTR

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Regulation of S-adenosylmethionine decarboxylase activity by alterations in the intracellular polyamine content

Cited by 58 publications

References 37 publications

BSCTV C2 Attenuates the Degradation of SAMDC1 to Suppress DNA Methylation-Mediated Gene Silencing in Arabidopsis

BSCTV C2 Attenuates the Degradation of SAMDC1 to Suppress DNA Methylation-Mediated Gene Silencing in Arabidopsis

S-Adenosylmethionine Decarboxylase Degradation by the 26 S Proteasome Is Accelerated by Substrate-mediated Transamination

Biological Effects of Polyamines on the Prevention of Aging-associated Diseases and on Lifespan Extension

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