Molecular and cellular characterization of GA-Stimulated Transcripts GASA4 and GASA6 in Arabidopsis thaliana

Copyright © 2016 Elsevier Ireland Ltd. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant science : an international journal of experimental plant biology. - 1985. - 246(2016) vom: 01. Mai, Seite 1-10
1. Verfasser: Qu, Jie (VerfasserIn)
Weitere Verfasser: Kang, Shin Gene, Hah, Cyrus, Jang, Jyan-Chyun
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2016
Zugriff auf das übergeordnete Werk:Plant science : an international journal of experimental plant biology
Schlagworte:Journal Article Research Support, Non-U.S. Gov't ABA GA Hormone crosstalk Peptide processing Signal peptide Arabidopsis Proteins GASA6 protein, Arabidopsis Gibberellins mehr... Plant Growth Regulators Protein Sorting Signals RNA, Messenger GASA protein, Arabidopsis 167679-73-4 Abscisic Acid 72S9A8J5GW
Beschreibung
Zusammenfassung:Copyright © 2016 Elsevier Ireland Ltd. All rights reserved.
GA and ABA play antagonistic roles in numerous cellular processes essential for growth, development, and stress responses. GASA4 and GASA6 belong to a family of GA-Stimulated transcripts in Arabidopsis, known as GA-inducible and ABA-repressible. We have found that GASA4 and GASA6 expression is likely mediated through a repressor of GA responses, GA INSENSITIVE (GAI) protein. Moreover, GASA4 and GASA6 are in general up regulated by growth hormones (auxin, BR, cytokinin, and GA) and down regulated by stress hormones (ABA, JA, and SA), indicating a role of GASA4 and GASA6 in hormone crosstalk. Genetic analyses show that suppression of both GASA4 and GASA6 causes late flowering, while over-expression of GASA6 causes early flowering in Arabidopsis. GASA family members encode small polypeptides sharing common structural features: an N-terminal signal peptide, a highly divergent intermediate region, and a conserved C-terminal domain containing 12 conserved cysteines. Despite the presence of a signal peptide, it has not been determined whether or not GASA4 and GASA6 can be processed in vivo. By using imaging and immunological analyses, we show that the N-terminal signal peptide is cleaved as predicted, and the cleavage is important for proper sub-cellular localization of GASA4 and GASA6
Beschreibung:Date Completed 14.12.2016
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2259
DOI:10.1016/j.plantsci.2016.01.009