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The ABA effect on the accumulation of an invertase inhibitor transcript that is driven by the CaMV35S promoter in Arabidopsis

Authors
Koh, Eun-JiLee, Sung JuneHong, Suk-WhanLee, Hoi SeonLee, Hojoung
Issue Date
30-9월-2008
Publisher
KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
Keywords
ABA; abiotic stress; Arabidopsis thaliana; invertase; invertase inhibitor; salt stress
Citation
MOLECULES AND CELLS, v.26, no.3, pp.236 - 242
Indexed
SCIE
SCOPUS
KCI
Journal Title
MOLECULES AND CELLS
Volume
26
Number
3
Start Page
236
End Page
242
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/122693
ISSN
1016-8478
Abstract
Invertase (beta-D-fructofuranosidase; EC 3.2.1.26) catalyzes the conversion of sucrose into glucose and fructose and is involved in an array of important processes, including phloem unloading, carbon partitioning, the response to pathogens, and the control of cell differentiation and development. Its importance may have caused the invertases to evolve into a multigene family whose members are regulated by a variety of different mechanisms, such as pH, sucrose levels, and inhibitor proteins. Although putative invertase inhibitors in the Arabidopsis genome are easy to locate, few studies have been conducted to elucidate their individual functions in vivo in plant growth and development because of their high redundancy. In this study we assessed the functional role of the putative invertase inhibitors in Arabidopsis by generating transgenic plants harboring a putative invertase inhibitor gene under the control of the CaMV35S promoter. A transgenic plant that expressed high levels of the putative invertase inhibitor transcript when grown under normal conditions was chosen for the current study. To our surprise, the stability of the invertase inhibitor transcripts was shown to be down-regulated by the phytohormone ABA (abscisic acid). It is well established that ABA enhances invertase activity in vivo but the underlying mechanisms are still poorly understood. Our results thus suggest that one way ABA regulates invertase activity is by down-regulating its inhibitor.
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