Yeast ornithine decarboxylase and antizyme form a 1:1 complex in vitro: Purification and characterization of the inhibitory complex

Chattopadhyay, Manas K.; Fernández, Cristina; Sharma, Deepak; McPhie, Peter; Masison, Daniel C.

doi:10.1016/j.bbrc.2011.01.113

Cited by 5 publications

(1 citation statement)

References 32 publications

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“…In yeast polyamine inhibition of polyamine synthesis by Az is a reversible process, suggested by the fact that heterodimer (Odc : Az) is inhibited when Odc is previously inactivated by DFMO [ 69 ]. Besides, this is the first report showing the 1 : 1 stoichiometric relation between Odc and Az.…”

Section: Regulation Of Polyamine Metabolismmentioning

confidence: 99%

Polyamine Metabolism in Fungi with Emphasis on Phytopathogenic Species

Valdés-Santiago

Cervantes-Chávez

León-Ramírez

et al. 2012

Journal of Amino Acids

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Polyamines are essential metabolites present in all living organisms, and this subject has attracted the attention of researchers worldwide interested in defining their mode of action in the variable cell functions in which they are involved, from growth to development and differentiation. Although the mechanism of polyamine synthesis is almost universal, different biological groups show interesting differences in this aspect that require to be further analyzed. For these studies, fungi represent interesting models because of their characteristics and facility of analysis. During the last decades fungi have contributed to the understanding of polyamine metabolism. The use of specific inhibitors and the isolation of mutants have allowed the manipulation of the pathway providing information on its regulation. During host-fungus interaction polyamine metabolism suffers striking changes in response to infection, which requires examination. Additionally the role of polyamine transporter is getting importance because of its role in polyamine regulation. In this paper we analyze the metabolism of polyamines in fungi, and the difference of this process with other biological groups. Of particular importance is the difference of polyamine biosynthesis between fungi and plants, which makes this process an attractive target for the control of phytopathogenic fungi.

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Section: Regulation Of Polyamine Metabolismmentioning

confidence: 99%

Polyamine Metabolism in Fungi with Emphasis on Phytopathogenic Species

Valdés-Santiago

Cervantes-Chávez

León-Ramírez

et al. 2012

Journal of Amino Acids

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Degrons of yeast and mammalian ornithine decarboxylase enzymes make potent combination for regulated targeted protein degradation

Joshi

Prabha

2016

Appl Microbiol Biotechnol

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Elevation of polyamine levels in eukaryotes leads to rapid degradation of ornithine decarboxylase (ODC), the first enzyme of polyamine biosynthesis pathway. ODC in yeast (yODC) has two domains, the Nα/β domain consisting of α/β barrel domain (α/β) preceded by an overhang of 50 residues at its N-terminus (N50) and β sheet domain at its C-terminus. Two degradation determinant signals or degrons in yODC sequence, namely the N50 and the antizyme-binding element (AzBE) housed in the α/β domain, are responsible for its degradation by proteasomes. Antizyme (Az) induced under polyamine excess binds to AzBE and delivers ODC to proteasome, while the N50 threads the protein into proteasome. It was previously reported by us that the peptide Nα/β of yODC acts as an independent transplantable degron, whose action can be modulated with the help of antizyme by varying polyamine levels. Mammalian ODC (mODC), in spite of its 40% sequence homology with yODC, is devoid of N50 of yODC and instead sports a C-terminal tail of 37 residues (CmODC). CmODC acts as an independent transplantable degron with no equivalent in yODC. The present study investigates the merits of employing the two degrons Nα/β and CmODC together for targeted protein degradation by expressing them in a chimeric fusion with green fluorescent protein (GFP). Our results establish that under the regulation of antizyme, the signals Nα/β and CmODC acting together enhance degradation better than either degron in isolation. The combination of Nα/β and CmODC can be employed to study the function of novel proteins through their rapid removal.

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