Plants contain two distinct classes of functional tryptophan synthase beta proteins

Ruohe Yin, Monika Frey, Alfons Gierl, Erich Glawischnig

Publikation: Beitrag in FachzeitschriftArtikelBegutachtung

15 Zitate (Scopus)

Abstract

Tryptophan synthase β-subunits (TSBs) catalyze the last step in tryptophan biosynthesis, i.e. The condensation of indole and serine yielding tryptophan. In microorganisms two subfamilies of TSBs (here designated as type 1 and type 2) are known, which are only distantly related. Surprisingly, in all genomes of multicellular plants analyzed genes encoding both types are present. While type 1 enzymes are well established as components of tryptophan synthase complexes, type 2 enzymes in plants have not yet been characterized. Tissue specific expression of the TSB genes from Arabidopsis thaliana was analyzed. While AtTSB1 is the predominantly expressed isoform in vegetative tissues, AtTSB1 and AtTSBtype2 reach similar transcript levels in seeds. AtTSBtype2 protein was expressed in Escherichia coli and purified. It converted indole and serine to tryptophan with a strikingly low Km-value for indole of ca. 74 nM. Attsbtype2 T-DNA insertion mutants showed no obvious deviation from the wild type phenotype, indicating that AtTSBtype2 function is not essential under standard growth conditions. As example for a monocot enzyme, maize TSB type 2 was analyzed and found to be transcribed in various tissues. ZmTSBtype2 was also catalytically active and here a Km-value for indole of ca. 7 μM was determined. These data indicate that TSB type 2 enzymes generally are functionally expressed in plants. Their potential biological role is discussed.

OriginalspracheEnglisch
Seiten (von - bis)1667-1672
Seitenumfang6
FachzeitschriftPhytochemistry
Jahrgang71
Ausgabenummer14-15
DOIs
PublikationsstatusVeröffentlicht - Okt. 2010

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