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Tissue-Specific Accumulation and Regulation of Zeaxanthin Epoxidase in Arabidopsis Reflect the Multiple Functions of the Enzyme in Plastids.
- Source :
-
Plant & Cell Physiology . Feb2015, Vol. 56 Issue 2, p346-357. 12p. - Publication Year :
- 2015
-
Abstract
- The enzyme zeaxanthin epoxidase (ZEP) catalyzes the conversion of zeaxanthin to violaxanthin, a key reaction for ABA biosynthesis and the xanthophyll cycle. Both processes are important for acclimation to environmental stress conditions, in particular drought (ABA biosynthesis) and light (xanthophyll cycle) stress. Hence, both ZEP functions may require differential regulation to optimize plant fitness. The key to understanding the function of ZEP in both stress responses might lie in its spatial and temporal distribution in plant tissues. Therefore, we analyzed the distribution of ZEP in plant tissues and plastids under drought and light stress by use of a ZEP-specific antibody. In addition, we determined the pigment composition of the plant tissues and chloroplast membrane subcompartments in response to these stresses. The ZEP protein was detected in all plant tissues (except flowers) concomitant with xanthophylls. The highest levels of ZEP were present in leaf chloroplasts and root plastids. Within chloroplasts, ZEP was localized predominantly in the thylakoid membrane and stroma, while only a small fraction was bound by the envelope membrane. Light stress affected neither the accumulation nor the relative distribution of ZEP in chloroplasts, while drought stress led to an increase of ZEP in roots and to a degradation of ZEP in leaves. However, drought stress-induced increases in ABA were similar in both tissues. These data support a tissue- and stress-specific accumulation of the ZEP protein in accordance with its different functions in ABA biosynthesis and the xanthophyll cycle. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00320781
- Volume :
- 56
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Plant & Cell Physiology
- Publication Type :
- Academic Journal
- Accession number :
- 101426944
- Full Text :
- https://doi.org/10.1093/pcp/pcu167