Subcellular localization of Arabidopsis arogenate dehydratases suggests novel and non-enzymatic roles

© The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 68(2017), 7 vom: 01. März, Seite 1425-1440
1. Verfasser: Bross, Crystal D (VerfasserIn)
Weitere Verfasser: Howes, Travis R, Abolhassani Rad, Sara, Kljakic, Ornela, Kohalmi, Susanne E
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2017
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arogenate dehydratase chloroplast division moonlighting proteins nuclear localization phenylalanine biosynthesis stromules. Arabidopsis Proteins Cyan Fluorescent Protein mehr... Green Fluorescent Proteins 147336-22-9 Hydro-Lyases EC 4.2.1.- pretyrosine dehydratase
Beschreibung
Zusammenfassung:© The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.
Arogenate dehydratases (ADTs) catalyze the final step in phenylalanine biosynthesis in plants. The Arabidopsis thaliana genome encodes a family of six ADTs capable of decarboxylating/dehydrating arogenate into phenylalanine. Using cyan fluorescent protein (CFP)-tagged proteins, the subcellular localization patterns of all six A. thaliana ADTs were investigated in intact Nicotiana benthamiana and A. thaliana leaf cells. We show that A. thaliana ADTs localize to stroma and stromules (stroma-filled tubules) of chloroplasts. This localization pattern is consistent with the enzymatic function of ADTs as many enzymes required for amino acid biosynthesis are primarily localized to chloroplasts, and stromules are thought to increase metabolite transport from chloroplasts to other cellular compartments. Furthermore, we provide evidence that ADTs have additional, non-enzymatic roles. ADT2 localizes in a ring around the equatorial plane of chloroplasts or to a chloroplast pole, which suggests that ADT2 is a component of the chloroplast division machinery. In addition to chloroplasts, ADT5 was also found in nuclei, again suggesting a non-enzymatic role for ADT5. We also show evidence that ADT5 is transported to the nucleus via stromules. We propose that ADT2 and ADT5 are moonlighting proteins that play an enzymatic role in phenylalanine biosynthesis and a second role in chloroplast division or transcriptional regulation, respectively
Beschreibung:Date Completed 18.07.2018
Date Revised 13.12.2023
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erx024