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Profiling the aminopropyltransferases in plants: their structure, expression and manipulation

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Abstract

Polyamines are organic polycations that are involved in a wide range of cellular activities related to growth, development, and stress response in plants. Higher polyamines spermidine and spermine are synthesized in plants and animals by a class of enzymes called aminopropyltransferases that transfer aminopropyl moieties (derived from decarboxylated S-adenosylmethionine) to putrescine and spermidine to produce spermidine and spermine, respectively. The higher polyamines show a much tighter homeostatic regulation of their metabolism than the diamine putrescine in most plants; therefore, the aminopropyltransferases are of high significance. We present here a comprehensive summary of the current literature on plant aminopropyltransferases including their distribution, biochemical properties, genomic organization, pattern of expression during development, and their responses to abiotic stresses, and manipulation of their cellular activity through chemical inhibitors, mutations, and genetic engineering. This minireview complements several recent reviews on the overall biosynthetic pathway of polyamines and their physiological roles in plants and animals. It is concluded that (1) plants often have two copies of the common aminopropyltransferase genes which exhibit redundancy of function, (2) their genomic organization is highly conserved, (3) direct enzyme activity data on biochemical properties of these enzymes are scant, (4) often there is a poor correlation among transcripts, enzyme activity and cellular contents of the respective polyamine, and (5) transgenic work mostly confirms the tight regulation of cellular contents of spermidine and spermine. An understanding of expression and regulation of aminopropyltransferases at the metabolic level will help us in effective use of genetic engineering approaches for the improvement in nutritional value and stress responses of plants.

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Abbreviations

Agm:

Agmatine

ADC:

Arginine decarboxylase

APT:

Aminopropyltransferase

Cad:

Cadaverine

CHA:

Cyclohexylamine

dcSAM:

Decarboxylated S-adenosylmethionine

DCHA:

Dicyclohexylamine

MTA:

5′-methylthioadenosine

ODC:

Ornithine decarboxylase

ORF:

Open reading frame

PA:

Polyamine

Put:

Putrescine

SAM:

S-adenosylmethionine

SAMDC:

S-adenosylmethionine decarboxylase

Spd:

Spermidine

SPDS:

Spermidine synthase

Spm:

Spermine

SPMS:

Spermine synthase

tSpm:

Thermospermine

tSPMS:

Thermospermine synthase

UTR:

Untranslated region

WT:

Wild type

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  1. Department of Biological Sciences, University of New Hampshire, Durham, NH, 03824, USA

    Lin Shao, Rajtilak Majumdar & Subhash C. Minocha

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  1. Lin Shao
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  2. Rajtilak Majumdar
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  3. Subhash C. Minocha
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Correspondence to Subhash C. Minocha.

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Scientific Contribution No. 2449 from the New Hampshire Agricultural Experiment Station.

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Shao, L., Majumdar, R. & Minocha, S.C. Profiling the aminopropyltransferases in plants: their structure, expression and manipulation. Amino Acids 42, 813–830 (2012). https://doi.org/10.1007/s00726-011-0998-8

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