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Molecular details of the Raptor-binding motif on Arabidopsis S6 kinase

Authors
Son, OraKim, SunghanHur, Yoon-SunCheon, Choong-Ill
Issue Date
Apr-2017
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords
AtRaptor1; Arabidopsis ribosomal S6 kinase 1; TOR; rDNA transcription
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.486, no.1, pp 137 - 142
Pages
6
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume
486
Number
1
Start Page
137
End Page
142
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/8604
DOI
10.1016/j.bbrc.2017.03.013
ISSN
0006-291X
1090-2104
Abstract
A putative raptor-binding fragment was identified from Arabidopsis S6 kinase 1 (AtS6K1) N-terminal domain in our previous study. Here, we report a further characterization of this fragment, which identified a 12-amino acid core element absolutely required for the interaction. Although the amino acid sequence of the element per se had no significant homology with the canonical consensus of the TOS (TOR-signaling) motif found in the mammalian TOR (target of rapamycin) kinase substrates, its overall sequence composition is similar to that of the TOS motif in that the acidic and non-polar amino acids residues are arranged in alternating fashion and having one or two of the bulky hydrophobic amino acid (F) buried in the interior. Substitution of this bulky residue completely abolished the binding of the fragment to AtRaptor1, as in the case of the mammalian TOS motif. Taken together with its position relative to the catalytic domain of the kinase, which also shows a resemblance with the TOS motif, these results appear to suggest that this core binding element in the N-terminus of AtS6K1 represents a plant version of the TOS motif. (C) 2017 Elsevier Inc. All rights reserved.
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이과대학 > 생명시스템학부 > 1. Journal Articles

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이과대학 (생명시스템학부)
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