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

Content Provider	Springer Nature Link
Author	Shao, Lin Majumdar, Rajtilak Micha, Subhash C.
Copyright Year	2011
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.
Starting Page	813
Ending Page	830
Page Count	18
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	42
Issue Number	2-3
e-ISSN	14382199
Language	English
Publisher	Springer Vienna
Publisher Date	2011-08-23
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	Polyamines Spermidine synthase Spermine synthase Transgenic manipulation Genetic manipulation Putrescine Neurobiology Life Sciences Biochemistry Proteomics Biochemical Engineering Analytical Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

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