Kelch-motif containing acyl-CoA binding proteins AtACBP4 and AtACBP5 are differentially expressed and function in floral lipid metabolism

Kelch-motif containing acyl-CoA binding proteins AtACBP4 and AtACBP5 are differentially expressed... Plant Mol Biol (2017) 93:209–225 DOI 10.1007/s11103-016-0557-5 Kelch-motif containing acyl-CoA binding proteins AtACBP4 and AtACBP5 are differentially expressed and function in floral lipid metabolism 1 2 2 2 1 Zi-Wei Ye  · Jie Xu  · Jianxin Shi  · Dabing Zhang  · Mee-Len Chye   Received: 22 February 2016 / Accepted: 30 October 2016 / Published online: 8 November 2016 © Springer Science+Business Media Dordrecht 2016 Abstract acbp4acbp5 buds, respectively, over Col-0. Analysis of Key message We herein demonstrated two of the inflorescences from acbp4 and acbp5 revealed that there Arabidopsis acyl-CoA-binding proteins (ACBPs), was an increase of AtACBP5 expression in acbp4, and an AtACBP4 and AtACBP5, both function in floral lipid increase of AtACBP4 expression in acbp5. Deletion anal- metabolism and they may possibly play complemen- ysis of the AtACBP4 and AtACBP5 5′-flanking regions tary roles in Arabidopsis microspore-to-pollen develop- indicated the minimal promoter activity for AtACBP4 ment. Histological analysis on transgenic Arabidopsis (−145/+103) and AtACBP5 (−181/+81). Electrophoretic expressing β-glucuronidase driven from the AtACBP4 mobility shift assays identified a pollen-specific cis-act- and AtACBP5 promoters, as well as, qRTPCR analysis ing element POLLEN1 (AGAAA) mapped at AtACBP4 revealed that AtACBP4 was expressed at stages 11–14 (−157/−153) which interacted with nuclear proteins in the mature pollen, while AtACBP5 was http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Kelch-motif containing acyl-CoA binding proteins AtACBP4 and AtACBP5 are differentially expressed and function in floral lipid metabolism

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Publisher
Springer Netherlands
Copyright
Copyright © 2016 by Springer Science+Business Media Dordrecht
Subject
Life Sciences; Plant Sciences; Biochemistry, general; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1007/s11103-016-0557-5
Publisher site
See Article on Publisher Site

Abstract

Plant Mol Biol (2017) 93:209–225 DOI 10.1007/s11103-016-0557-5 Kelch-motif containing acyl-CoA binding proteins AtACBP4 and AtACBP5 are differentially expressed and function in floral lipid metabolism 1 2 2 2 1 Zi-Wei Ye  · Jie Xu  · Jianxin Shi  · Dabing Zhang  · Mee-Len Chye   Received: 22 February 2016 / Accepted: 30 October 2016 / Published online: 8 November 2016 © Springer Science+Business Media Dordrecht 2016 Abstract acbp4acbp5 buds, respectively, over Col-0. Analysis of Key message We herein demonstrated two of the inflorescences from acbp4 and acbp5 revealed that there Arabidopsis acyl-CoA-binding proteins (ACBPs), was an increase of AtACBP5 expression in acbp4, and an AtACBP4 and AtACBP5, both function in floral lipid increase of AtACBP4 expression in acbp5. Deletion anal- metabolism and they may possibly play complemen- ysis of the AtACBP4 and AtACBP5 5′-flanking regions tary roles in Arabidopsis microspore-to-pollen develop- indicated the minimal promoter activity for AtACBP4 ment. Histological analysis on transgenic Arabidopsis (−145/+103) and AtACBP5 (−181/+81). Electrophoretic expressing β-glucuronidase driven from the AtACBP4 mobility shift assays identified a pollen-specific cis-act- and AtACBP5 promoters, as well as, qRTPCR analysis ing element POLLEN1 (AGAAA) mapped at AtACBP4 revealed that AtACBP4 was expressed at stages 11–14 (−157/−153) which interacted with nuclear proteins in the mature pollen, while AtACBP5 was

Journal

Plant Molecular BiologySpringer Journals

Published: Nov 8, 2016

References

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