Autoregulatory Frameshifting in Antizyme Gene Expression Governs Polyamine Levels from Yeast to Mammals

Ivanov, Ivaylo P.; Matsufuji, Senya

doi:10.1007/978-0-387-89382-2_13

Cited by 6 publications

(9 citation statements)

References 80 publications

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“…It targets specific proteins for ubiquitin-independent proteosomal-mediated degradation. Its best known interaction is with ornithine decarboxylase that catalyzes synthesis of putrescene, the precursor of the polyamines spermidine and spermine ( 7 – 9 ). In addition to inhibiting the synthesis of polyamines, antizyme also inhibits extra cellular uptake of polyamines ( 10 ) ( Fig.…”

Section: Introductionmentioning

confidence: 99%

A Nascent Peptide Signal Responsive to Endogenous Levels of Polyamines Acts to Stimulate Regulatory Frameshifting on Antizyme mRNA

Yordanova

Andreev

et al. 2015

Journal of Biological Chemistry

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Background: Regulatory +1 frameshifting in antizyme mRNA is central for polyamine level homeostasis.Results: A nascent peptide stimulator of +1 frameshifting operates in Agaricomycete fungal antizyme mRNA.Conclusion: Frameshifting can be stimulated by nascent peptide interactions with the ribosome's peptide exit tunnel in a polyamine-dependent manner.Significance: Specific nascent peptide stimulators may be a more general and unappreciated feature of utilized ribosomal frameshifting.

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Section: Introductionmentioning

confidence: 99%

A Nascent Peptide Signal Responsive to Endogenous Levels of Polyamines Acts to Stimulate Regulatory Frameshifting on Antizyme mRNA

Yordanova

Andreev

et al. 2015

Journal of Biological Chemistry

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“…The core sequence similarity match of the domains is 100% and matrix similarity is greater than 90%. Antizyme frameshifting efficiency was often enhanced by the presence of cisacting elements, both 5′ and 3′ of the frameshifting site (Ivanov and Matsufuji, 2010). We found that one typical element, the TATA box (TATA AA) was at −24 to −29.…”

Section: Detection Of Snp and Putative Cis-acting Elements In The Pormentioning

confidence: 81%

“…We found that the porcine AZ1 gene was expressed in all the examined tissues, and in highest amount in lung, then cardiac muscle, liver, and backfat, low in other porcine tissues. Previous studies showed that AZ1 mRNA is expressed stably in many tissues of human (Ivanov and Matsufuji, 2010) and rat (Matsufuji et al, 1990). In humans, the gene is highly expressed in skeletal muscle, cardiac muscle, and brain, and exhibits low expression levels in lung, liver, and kidney (Ivanov and Matsufuji, 2010).…”

Section: Tissue Expression Pattern Of the Porcine Az1 Genementioning

confidence: 99%

“…Previous studies showed that AZ1 mRNA is expressed stably in many tissues of human (Ivanov and Matsufuji, 2010) and rat (Matsufuji et al, 1990). In humans, the gene is highly expressed in skeletal muscle, cardiac muscle, and brain, and exhibits low expression levels in lung, liver, and kidney (Ivanov and Matsufuji, 2010). In zebrafish, one novel antizyme gene, which does not correspond to any of the known orthologous groups in vertebrates, was expressed in the retinal ganglion cell layer of the eye, and in the brain and somites .…”

Section: Tissue Expression Pattern Of the Porcine Az1 Genementioning

confidence: 99%

“…Antizyme 3 is expressed specifically in late spermatocytes and early spermatids (Ivanov et al, 2000a(Ivanov et al, , 2000bTosaka et al, 2000). Antizyme regulates ODC tightly and negatively, and mediates a bifurcated response to polyamine levels (Coffino, 2001;Ivanov and Matsufuji, 2010). Antizyme binds to ODC and targets it for degradation by 26S proteasomes (Coffino, 2001;Murakami et al, 1992;Zhang et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

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Molecular characterization, tissue expression and nucleotide variation of the porcine AZ1 gene

Zhang

et al. 2012

Gene

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Subcellular localization and phosphorylation of antizyme 2

Murai

Shimizu

Murakami

et al. 2009

J of Cellular Biochemistry

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Antizymes (AZs) are polyamine-induced proteins that negatively regulate cellular polyamine synthesis and uptake. Three antizyme isoforms are conserved among mammals. AZ1 and AZ2 have a broad tissue distribution, while AZ3 is testis specific. Both AZ1 and AZ2 inhibit ornithine decarboxylase (ODC) activity by binding to ODC monomer and target it to the 26S proteasome at least in vivo. Both also inhibit extra-cellular polyamine uptake. Despite their being indistinguishable by these criteria, we show here using enhanced green fluorescent protein (EGFP)-AZ2 fusion protein that in mammalian cells, the subcellular location of AZ2 is mainly in the nucleus, and is different from that of AZ1. The C-terminal part of AZ2 is necessary for the nuclear distribution. Within a few hours, a shift in the distribution of EGFP-AZ2 fusion protein from cytoplasm to the nucleus or from nucleus to cytoplasm is observable in NIH3T3 cells. In addition, we found that in cells a majority of AZ2, but not AZ1, is phosphorylated at Ser-186, likely by protein kinase CK2. There may be a specific function of AZ2 in the nucleus.

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Autoregulatory Frameshifting in Antizyme Gene Expression Governs Polyamine Levels from Yeast to Mammals

Cited by 6 publications

References 80 publications

A Nascent Peptide Signal Responsive to Endogenous Levels of Polyamines Acts to Stimulate Regulatory Frameshifting on Antizyme mRNA

A Nascent Peptide Signal Responsive to Endogenous Levels of Polyamines Acts to Stimulate Regulatory Frameshifting on Antizyme mRNA

Molecular characterization, tissue expression and nucleotide variation of the porcine AZ1 gene

Subcellular localization and phosphorylation of antizyme 2

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