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Salt bridge in the conserved His-Asp cluster in Gloeobacter rhodopsin contributes to trimer formation

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/52199

Title: Salt bridge in the conserved His-Asp cluster in Gloeobacter rhodopsin contributes to trimer formation
Authors: Tsukamoto, Takashi Browse this author
Kikukawa, Takashi Browse this author →KAKEN DB
Kurata, Takuro Browse this author
Jung, Kwang-Hwan Browse this author
Kamo, Naoki Browse this author
Demura, Makoto Browse this author →KAKEN DB
Keywords: Microbial rhodopsin
Histidine-Aspartate cluster
Quaternary structure
Protonation
Size-exclusion chromatography
Circular dichroism spectroscopy
Issue Date: 14-Feb-2013
Publisher: Elsevier B.V.
Journal Title: FEBS Letters
Volume: 587
Issue: 4
Start Page: 322
End Page: 327
Publisher DOI: 10.1016/j.febslet.2012.12.022
PMID: 23313943
Abstract: Gloeobacter rhodopsin (GR) is a eubacterial proton pump having a highly conserved histidine near the retinal Schiff base counter-ion, aspartate. Various interactions between His and Asp of the eubacterial proton pump have been reported. Here, we showed the pH-dependent trimer/monomer transition of GR in the presence of dodecyl-β-D-maltoside by size-exclusion chromatography. The pH dependence was closely related to the protonation state of the counter-ion, Asp121. For the H87M mutant, pH dependence disappeared and a monomer became dominant. We concluded that the formation or breaking of the salt bridge between His87 and Asp121 inside the protein changes the quaternary structure.
Type: article (author version)
URI: http://hdl.handle.net/2115/52199
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 出村 誠

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