2008, Number 1-2
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Microbiología 2008; 50 (1-2)
Indole-acetic acid production in Azospirillum
Aguilar-Piedras JJ, Xiqui-Vásquez ML, García-García S, Baca BE
Language: Spanish
References: 60
Page: 29-37
PDF size: 158.01 Kb.
ABSTRACT
Azospirillum is a free-nitrogen fixing bacterium, isolated from rhizosphere and intracellular spaces of the roots of several plants. Numerous reports have shown the improvement of plant growth and crop yield upon
Azospirillum inoculation to plants. The observed plant response to
Azospirillum has been attributed to several mechanisms that could be operating simultaneously, among them the production of indole-3-acetic acid (IAA) by the bacterium. This review considers the complex biosynthetic production of IAA in
Azospirillum. Three tryptophan-dependent pathways, which are generally named after an intermediate, have been proposed to be occurring in
Azospirillum. The indole-3-pyruvic acid (IPyA) route which is likely the most important, the tryptamine pathway, and the indole-3-acetonitrile route, and one pathway Trp-independent using an indolic Trp precursor; however none of them are fully elucidated. Biochemical studies showed two aromatic aminoransferases (AATs) enzymatic activity from
A. brasilense and four from
A. lipoferum, which could be involved in IPyA synthesis. The ipdC gene coding the key enzyme phenyl-3-pyruvate decarboxylase (PPDC) of IPyA pathway was identified from several strains. Interestingly, ipdC from
A. brasilense Sp245 strain is up regulated by IAA, and all genes ipdC identified are expressed in association with the plant. The anthranilate synthase catalyzing the conversion of chorismate to anthranilate which. It is the initial reaction in Trp biosynthesis codified by trpE(G), and two copies occur in
A. brasilense genome. It was demonstrated that both trpE(G) genes participate in IAA synthesis and are differentially regulated. Therefore,
A. brasilense has a plenty pool of Trp for IAA synthesis. Other proteins play a role in IAA production such as the ClpX stress protein, as well as an outer membrane protein and a protein involved in transport of Fe
+3.
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