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Abstract Detail


Water Relations

Ko, Dae Kwan [1], cho, eun kyung [2], Hong, Choo Bong [3].

Functional analysis of heat shock protein 70 in flooding-stressed Nicotiana tabacum.

Heat shock protein 70 (HSP70)-based chaperone machinery is expected to play a pivotal role in plants under environmental stresses. Three genomic clones, NtHSP70-1, NtHSP70-2 and NtHSP70-3, coding tobacco HSP70s were isolated and analyzed for their expression patterns. Open reading frames of NtHSP70-1, NtHSP70-2, NtHSP70-3 were 653, 653 and 648 amino acid residues, respectively. They all shared three conserved regions, namely C-terminal substrate binding domain, oligomerization domain, and N-terminal ATPase domain. Among them, transcription of NtHSP70-3 was especially increased under flooding-stress in addition to heat shock condition. In light of recent reported results that define the cooperative functions of HSP70 and sHSPs under heat shock condition, there is a possibility that NtHSP70-3 interacts with sHSPs under flooding-stress condition.


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1 - Institute of Molecular Biology and Genetics, Department of Biological Sciences, Seoul National University, Plant Molecular Physiology Lab, seoul, 151-747, korea
2 - Institute of Marine Biotechnology Center, Department of Bio-Food Materials, Silla University, Busan, 617, Korea
3 - Institute of Molecular Biology and Genetics, Department of Biological Sciences, Seoul National University, Plant Molecular Phisiology Lab, seoul, 151, korea

Keywords:
heat shock protein
flooding.

Presentation Type: Plant Biology Abstract
Session: P
Location: Exhibit Hall (Northeast, Southwest & Southeast)/Hilton
Date: Sunday, July 8th, 2007
Time: 8:00 AM
Number: P09011
Abstract ID:844


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