Barley DNA-binding methionine aminopeptidase, which changes the localization from the nucleus to the cytoplasm by low temperature, is involved in freezing tolerance

Copyright © 2010 Elsevier Ireland Ltd. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant science : an international journal of experimental plant biology. - 1985. - 180(2011), 1 vom: 03. Jan., Seite 53-60
1. Verfasser: Jeong, Hee-Jeong (VerfasserIn)
Weitere Verfasser: Shin, Jeong Sheop, Ok, Sung Han
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2011
Zugriff auf das übergeordnete Werk:Plant science : an international journal of experimental plant biology
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Plant Proteins Abscisic Acid 72S9A8J5GW Aminopeptidases EC 3.4.11.- Methionyl Aminopeptidases EC 3.4.11.18
Beschreibung
Zusammenfassung:Copyright © 2010 Elsevier Ireland Ltd. All rights reserved.
The polymerase chain reaction-based Mirror Orientation Selection (MOS) method was used to isolate low temperature-induced genes from cold-treated winter barley (Hordeum vulgare L. cv. Dongbori). MOS screening identified a novel methionine (Met) aminopeptidase (MAP) designated as HvMAP. The deduced HvMAP protein was determined to possess an aminopeptidase domain and a nuclear localization signal. An in vitro enzyme assay using recombinant HvMAP protein demonstrated MAP activity. The expression of this gene was induced by low temperature and abscisic acid treatment, and overexpression of this gene conferred stronger freezing tolerance to Arabidopsis transgenic plants as compared to wild-type plants. Interestingly, low temperature treatment changed the localization of HvMAP from the nucleus to the cytoplasm. These findings suggest that HvMAP is a novel MAP that functions in freezing tolerance by facilitating protein maturation
Beschreibung:Date Completed 05.07.2011
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2259
DOI:10.1016/j.plantsci.2010.09.004