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GrainGenes Reference Report: TPJ-40-410

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Reference	TPJ-40-410
Title	A novel C-terminal sequence from barley polyamine oxidase is a vacuolar sorting signal
Journal	Plant Journal
Year	2004
Volume	40
Pages	410-418
Author	Cervelli M [ Show all 7 ]
Abstract	Barley contains two different isoforms of flavin-containing polyamine oxidase (BPAO1 and BPAO2). We have previously demonstrated that BPAO2 is a symplastic protein in barley leaves. On the contrary, maize polyamine oxidase (MPAO), the best characterized member of this enzyme class, is apoplastic. Comparison of the derived amino-acid sequences of BPAO2 and MPAO has revealed that both precursor proteins include a cleavable N-terminal signal peptide of 25 amino acid residues, but the barley enzyme shows an extra C-terminal extension of eight amino acids. By means of MPAO engineering with BPAO2 C-terminal tail (MPAO-T) and exploiting transient expression in Nicotiana tabacum protoplasts, we demonstrate that this oligopeptide is a signal for protein sorting to the plant vacuole. The vacuolar sorting of MPAO-T was saturable. Specific mutations of the C-terminal tail were constructed to determine which amino acid residues of this novel propeptide affect proper protein sorting. No consensus sequence or common structural determinant is required for the intracellular retention of the MPAO-T protein, but a gradual lowering of the efficiency was observed as a result of progressive deletion of the C-terminus
Keyword	[ Hide all but 1 of 29 ] amino acid sequences amino acids barley corn flavoproteins grain crops Hordeum vulgare isozymes leaves maize molecular sequence data mutations Nicotiana tabacum nucleotide sequences oxidoreductases plant proteins polyamine oxidase post-translational modification protein secretion proteins protoplasts recombinant fusion proteins signal peptide tail tobacco transgenic plants vacuolar sorting signal vacuoles Zea mays

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