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Probing protein structural requirements for activation of membrane-bound NAC transcription factors in Arabidopsis and rice

Cited 10 time in Web of Science Cited 11 time in Scopus
Authors
Kim, Sang-Gyu; Lee, Sangmin; Ryu, Jaeyong; Park, Chung-Mo
Issue Date
2010-03
Citation
Plant Science, Vol.178 No.3, pp.239-244
Keywords
ArabidopsisHydrophobicityMTFNTLTranscription factor
Abstract
Many transcription factors are stored in a dormant state through association with the cellular membranes in plants Upon stimulation by internal and environmental signals, they are activated through proteolytic cleavage events either by membrane-associated proteases or by ubiquitination-dependent proteasome activities Controlled proteolytic activation of the dormant, membrane-bound transcription factors (MTFs) is an intriguing way of ensuring rapid transcriptional responses to abrupt environmental changes However, the underlying activation mechanisms and protein structural requirements are largely unknown in most cases Here, we analyzed the primary and secondary structures of the NAC MTFs, particularly of the amino acid sequences surrounding the putative cleavage sites Interestingly, the putative biologically active forms have strong hydrophilic motifs at their C-termini. Accordingly, transgenic Arabidopsis plants overexpressing the truncated forms having the C-terminal hydrophilic motifs exhibited distinct phenotypes. The finding was also applicable to rice NAC MTFs Among the full-size OsNTL2 protein and a series of truncated OsNTL2 forms lacking the C-terminal transmembrane motif, only the OsNTL2 form (Os2 Delta C4) having a strong hydrophilic peak at the C-terminus exhibited a high tianscriptional activation activity when assayed in yeast cells Our findings will provide insights into how plant MTFs are activated to release the biologically active forms (C) 2010 Elsevier Ireland Ltd All rights reserved.
ISSN
0168-9452
URI
https://hdl.handle.net/10371/172060
DOI
https://doi.org/10.1016/j.plantsci.2009.12.007
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College of Natural Sciences (자연과학대학)Dept. of Chemistry (화학부)Journal Papers (저널논문_화학부)
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