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Temperature controls nuclear import of Tam3 transposase in Antirrhinum

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/47949

Title: Temperature controls nuclear import of Tam3 transposase in Antirrhinum
Authors: Fujino, Kaien Browse this author
Hashida, Shin-nosuke Browse this author
Ogawa, Takashi Browse this author
Natsume, Tomoko Browse this author
Uchiyama, Takako Browse this author
Mikami, Tetsuo Browse this author
Kishima, Yuji Browse this author →KAKEN DB
Keywords: low-temperature-dependent transposition (LTDT)
nuclear import
transposase (TPase)
transposon Tam3
Antirrhinum majus
Issue Date: Jan-2011
Publisher: Wiley-Blackwell
Journal Title: The Plant Journal
Volume: 65
Issue: 1
Start Page: 146
End Page: 155
Publisher DOI: 10.1111/j.1365-313X.2010.04405.x
PMID: 21175897
Abstract: It has been proposed that environmental stimuli can activate transposable elements (TEs), while few substantial mechanisms have been shown so far. The class II element Tam3 from Antirrhinum majus exhibits a unique property of low-temperature-dependent transposition (LTDT). LTDT has proved invaluable in developing the gene isolation technologies that have underpinned much of modern plant developmental biology. Here, we reveal that LTDT involves differential sub-cellular localization of the Tam3 transposase (TPase) in cells grown at low (15℃) and high (25℃) temperatures. The mechanism is associated with the nuclear import of Tam3 TPase in Antirrhinum cells. At high temperature, the nuclear import of Tam3 TPase is severely restricted in Antirrhinum cells, while at low temperature, the nuclear localization of Tam3 TPase is observed in about 20% of the cells. However, in tobacco BY-2 and onion cells, Tam3 TPase is transported into most nuclei. In addition to three nuclear localization signals (NLSs), the Tam3 TPase is equipped with a nuclear localization inhibitory domain (NLID), which functions to abolish nuclear import of the TPase at high temperature in Antirrhinum. NLID in Tam3 TPase is considered to interact with Antirrhinum specific factor(s). The host-specific regulation of the nuclear localization of transposase represents a new repertoire controlling class II TEs.
Rights: The definitive version is available at www.blackwell-synergy.com
Type: article (author version)
URI: http://hdl.handle.net/2115/47949
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 貴島 祐治

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