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Title: Imbalance of tyrosine by modulating TyrA arogenate dehydrogenases impacts growth and development of Arabidopsis thaliana
Summary

l‐Tyrosine is an essential aromatic amino acid required for the synthesis of proteins and a diverse array of plant natural products; however, little is known on how the levels of tyrosine are controlledin plantaand linked to overall growth and development. Most plants synthesize tyrosine by TyrA arogenate dehydrogenases, which are strongly feedback‐inhibited by tyrosine and encoded byTyrA1andTyrA2genes inArabidopsis thaliana. While TyrA enzymes have been extensively characterized at biochemical levels, theirin plantafunctions remain uncertain. Here we found thatTyrA1suppression reduces seed yield due to impaired anther dehiscence, whereasTyrA2knockout leads to slow growth with reticulate leaves. Thetyra2mutant phenotypes were exacerbated byTyrA1suppression and rescued by the expression ofTyrA2,TyrA1or tyrosine feeding. Low‐light conditions synchronized thetyra2and wild‐type growth, and ameliorated thetyra2leaf reticulation. After shifting to normal light,tyra2transiently decreased tyrosine and subsequently increased aspartate before the appearance of the leaf phenotypes. Overexpression of the deregulated TyrA enzymes led to hyper‐accumulation of tyrosine, which was also accompanied by elevated aspartate and reticulate leaves. These results revealed that TyrA1 and TyrA2 have distinct and overlapping functions in flower and leaf development, respectively, and that imbalance of tyrosine, caused by altered TyrA activity and regulation, impacts growth and development of Arabidopsis. The findings provide critical bases for improving the production of tyrosine and its derived natural products, and further elucidating the coordinated metabolic and physiological processes to maintain tyrosine levels in plants.

 
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NSF-PAR ID:
10083546
Author(s) / Creator(s):
 ;  ;  ;  ;  ;  
Publisher / Repository:
Wiley-Blackwell
Date Published:
Journal Name:
The Plant Journal
Volume:
97
Issue:
5
ISSN:
0960-7412
Page Range / eLocation ID:
p. 901-922
Format(s):
Medium: X
Sponsoring Org:
National Science Foundation
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