Binding interactions of the peripheral stalk subunit isoforms from human V-ATPase-Reference-Cited by-同舟云学术

Binding interactions of the peripheral stalk subunit isoforms from human V-ATPase

Published:2016-05-03 Issue:5 Volume:80 Page:878-890
ISSN:0916-8451
Container-title:Bioscience, Biotechnology, and Biochemistry
language:en
Short-container-title:

Author:

Rahman Suhaila¹,Yamato Ichiro¹,Saijo Shinya¹,Mizutani Kenji¹²,Takamuku Yuuki²,Ishizuka-Katsura Yoshiko³,Ohsawa Noboru³,Terada Takaho³,Shirouzu Mikako³,Yokoyama Shigeyuki³⁴,Murata Takeshi²³⁵⁶

Affiliation:

1. Department of Biological Science and Technology, Tokyo University of Science, Tokyo, Japan

2. Department of Chemistry, Graduate School of Science, Chiba University, Chiba, Japan

3. RIKEN Systems and Structural Biology Center, Yokohama, Japan

4. Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Tokyo, Japan

5. Molecular Chirality Research Center, Chiba University, Chiba, Japan

6. JST, PRESTO, Chiba, Japan

Abstract

Abstract The mammalian peripheral stalk subunits of the vacuolar-type H+-ATPases (V-ATPases) possess several isoforms (C1, C2, E1, E2, G1, G2, G3, a1, a2, a3, and a4), which may play significant role in regulating ATPase assembly and disassembly in different tissues. To better understand the structure and function of V-ATPase, we expressed and purified several isoforms of the human V-ATPase peripheral stalk: E1G1, E1G2, E1G3, E2G1, E2G2, E2G3, C1, C2, H, a1NT, and a2NT. Here, we investigated and characterized the isoforms of the peripheral stalk region of human V-ATPase with respect to their affinity and kinetics in different combination. We found that different isoforms interacted in a similar manner with the isoforms of other subunits. The differences in binding affinities among isoforms were minor from our in vitro studies. However, such minor differences from the binding interaction among isoforms might provide valuable information for the future structural-functional studies of this holoenzyme.

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

Link

http://academic.oup.com/bbb/article-pdf/80/5/878/36829439/bbb0878.pdf

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