Solution structure and dynamics of mouse ARMET

Edited by Judit Ovádi

Received 16 February 2010; received in revised form 16 February 2010; accepted 2 March 2010. published online 08 March 2010.

Abstract

ARMET is an endoplasmic reticulum (ER) stress-inducible protein that is required for maintaining cell viability under ER stress conditions. However, the exact molecular mechanisms by which ARMET protects cells are unknown. Here, we have analyzed the solution structure of ARMET. ARMET has an entirely α-helical structure, which is composed of two distinct domains. Positive charges are dispersed on the surfaces of both domains and across a linker structure. Trypsin digestion and 15N relaxation experiments indicate that the tumbling of the N-terminal and C-terminal domains is effectively independent. These results suggest that ARMET may hold a negatively charged molecule using the two positively charged domains.

Keywords: ER stress, Solution structure, Positive charge, Domain movement

a Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, 53 Kawahara-cho, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan

b Graduate School of Pharmaceutical Sciences, Nagoya City University, Tanabe-dori 3-1, Mizuho-ku, Nagoya 467-8603, Japan

c Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Japan

d Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Japan

Corresponding author. Fax: +81 75 751 4645.

1 Present address: Structural Glycobiology Team, Systems Glycobiology Research Group, Chemical Biology Department, RIKEN, Advanced Science Institute, 2-1 Hirosawa Wako, Saitama 351-0198, Japan.

2 Present address: Department of Life Science, Faculty of Engineering and Resource Science, Akita University, Akita 010-8502, Japan.

PII: S0014-5793(10)00202-4

doi:10.1016/j.febslet.2010.03.008

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