Accumulation of the transcription factor ABA-insensitive (ABI)4 is tightly regulated post-transcriptionally

ABA-INSENSITIVE (ABI)4 is a transcription factor implicated in response to ABA in maturing seeds, and seedling responses to ABA, salt, and sugar. Previous studies have shown that ABI4 transcripts are high in seeds and in seedlings exposed to high concentrations of glucose and, to a lesser extent, os...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 62(2011), 11 vom: 01. Juli, Seite 3971-9
1. Verfasser: Finkelstein, Ruth (VerfasserIn)
Weitere Verfasser: Lynch, Tim, Reeves, Wendy, Petitfils, Michelle, Mostachetti, Mike
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2011
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. ABI4 protein, Arabidopsis Arabidopsis Proteins Plant Growth Regulators Plant Proteins Transcription Factors Green Fluorescent Proteins 147336-22-9 mehr... Abscisic Acid 72S9A8J5GW Glucuronidase EC 3.2.1.31
Beschreibung
Zusammenfassung:ABA-INSENSITIVE (ABI)4 is a transcription factor implicated in response to ABA in maturing seeds, and seedling responses to ABA, salt, and sugar. Previous studies have shown that ABI4 transcripts are high in seeds and in seedlings exposed to high concentrations of glucose and, to a lesser extent, osmotic agents and ABA, but that transcript levels are very low through most of vegetative growth. This study examined ABI4 protein accumulation indirectly, using transgenic lines expressing fusions to GFP and GUS. The GFP fusions were active, but undetectable visually or immunologically. Comparison of transcript and activity levels for GUS expression showed that inclusion of the ABI4 coding sequence reduced the ratio of activity to transcript ∼40-fold when driven by the CaMV 35S promoter, and nearly 150-fold when controlled by the ABI4 promoter. At least part of this discrepancy is due to proteasomal degradation of ABI4, resulting in a half-life of 5-6 h for the ABI4-GUS fusion. Comparison of the spatial localization of transcripts and fusion proteins indicated that the protein preferentially accumulated in roots such that transcript and protein distribution had little similarity. The components mediating targeting to the proteasome or other mechanisms of spatial restriction have not yet been identified, but several domains of ABI4 appear to contribute to its instability
Beschreibung:Date Completed 07.11.2011
Date Revised 20.10.2021
published: Print-Electronic
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/err093