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AtFTCD-L, a trans-Golgi network localized protein, modulates root growth of Arabidopsis in high-concentration agar culture medium.
- Source :
- Planta: An International Journal of Plant Biology; Jul2022, Vol. 256 Issue 1, p1-13, 13p
- Publication Year :
- 2022
-
Abstract
- Main conclusion: AtFTCD-L protein is localized on the TGN vesicles in Arabidopsis root cap cells. AtFTCD-L mutation resulted in slow root growth of Arabidopsis in high-concentration agar culture medium. Arabidopsis formiminotransferase cyclodeaminase-like protein (AtFTCD-L) in Arabidopsis is homologous to the formiminotransferase cyclodeaminase (FTCD) protein in animal cells. However, the localization and function of AtFTCD-L remain unknown in Arabidopsis. In this study, we generated and analyzed a deletion mutant of AtFTCD-L with a T-DNA insertion. We found that the growth of Arabidopsis roots with the T-DNA insertion mutation in AtFTCD-L was slower than that of wild-type roots when grown in high-concentration 1/2 MS agar culture medium. AtFTCD-L-GFP could restore the ftcd-l mutant phenotype. In addition, the AtFTCD-L protein was localized on the trans-Golgi network (TGN) vesicles in Arabidopsis root cap cells. Fluorescence recovery after photobleaching (FRAP) experiment using Arabidopsis pollen-specific receptor-like kinase-GFP (AtPRK1-GFP) stably transformed plants showed that the deficiency of AtFTCD-L protein in Arabidopsis led to slower secretion in the root cap peripheral cells. The AtFTCD-L protein deficiency also resulted in a significantly reduced monosaccharides content in the culture medium. Based on the above results, we speculate that the AtFTCD-L protein may be involved in sorting and/or transportation of TGN vesicles in root cap peripheral cells, thereby regulating the extracellular secretion of mucilage components in the root cap. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00320935
- Volume :
- 256
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- Planta: An International Journal of Plant Biology
- Publication Type :
- Academic Journal
- Accession number :
- 157452645
- Full Text :
- https://doi.org/10.1007/s00425-022-03911-5