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Mutant LV(476-7)AA of A-subunit of Enterococcus hirae V(1)-ATPase: High affinity of A(3)B(3) complex to DF axis and low ATPase activity
Vacuolar ATPase (V-ATPase) of Enterococcus hirae is composed of a soluble functional domain V(1) (A(3)B(3)DF) and an integral membrane domain V(o) (ac), where V(1) and V(o) domains are connected by a central stalk, composed of D-, F-, and d-subunits; and two peripheral stalks (E- and G-subunits). We...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3879392/ https://www.ncbi.nlm.nih.gov/pubmed/24404436 http://dx.doi.org/10.1186/2193-1801-2-689 |
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author | Alam, Jahangir Yamato, Ichiro Arai, Satoshi Saijo, Shinya Mizutani, Kenji Ishizuka-Katsura, Yoshiko Ohsawa, Noboru Terada, Takaho Shirouzu, Mikako Yokoyama, Shigeyuki Iwata, So Kakinuma, Yoshimi Murata, Takeshi |
author_facet | Alam, Jahangir Yamato, Ichiro Arai, Satoshi Saijo, Shinya Mizutani, Kenji Ishizuka-Katsura, Yoshiko Ohsawa, Noboru Terada, Takaho Shirouzu, Mikako Yokoyama, Shigeyuki Iwata, So Kakinuma, Yoshimi Murata, Takeshi |
author_sort | Alam, Jahangir |
collection | PubMed |
description | Vacuolar ATPase (V-ATPase) of Enterococcus hirae is composed of a soluble functional domain V(1) (A(3)B(3)DF) and an integral membrane domain V(o) (ac), where V(1) and V(o) domains are connected by a central stalk, composed of D-, F-, and d-subunits; and two peripheral stalks (E- and G-subunits). We identified 120 interacting residues of A(3)B(3) heterohexamer with D-subunit in DF heterodimer in the crystal structures of A(3)B(3) and A(3)B(3)DF. In our previous study, we reported 10 mutants of E. hirae V(1)-ATPase, which showed lower binding affinities of DF with A(3)B(3) complex leading to higher initial specific ATPase activities compared to the wild-type. In this study, we identified a mutation of A-subunit (LV(476-7)AA) at its C-terminal domain resulting in the A(3)B(3) complex with higher binding affinities for wild-type or mutant DF heterodimers and lower initial ATPase activities compared to the wild-type A(3)B(3) complex, consistent with our previous proposal of reciprocal relationship between the ATPase activity and the protein-protein binding affinity of DF axis to the A(3)B(3) catalytic domain of E. hirae V-ATPase. These observations suggest that the binding of DF axis at the contact region of A(3)B(3) rotary ring is relevant to its rotation activity. |
format | Online Article Text |
id | pubmed-3879392 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-38793922014-01-08 Mutant LV(476-7)AA of A-subunit of Enterococcus hirae V(1)-ATPase: High affinity of A(3)B(3) complex to DF axis and low ATPase activity Alam, Jahangir Yamato, Ichiro Arai, Satoshi Saijo, Shinya Mizutani, Kenji Ishizuka-Katsura, Yoshiko Ohsawa, Noboru Terada, Takaho Shirouzu, Mikako Yokoyama, Shigeyuki Iwata, So Kakinuma, Yoshimi Murata, Takeshi Springerplus Research Vacuolar ATPase (V-ATPase) of Enterococcus hirae is composed of a soluble functional domain V(1) (A(3)B(3)DF) and an integral membrane domain V(o) (ac), where V(1) and V(o) domains are connected by a central stalk, composed of D-, F-, and d-subunits; and two peripheral stalks (E- and G-subunits). We identified 120 interacting residues of A(3)B(3) heterohexamer with D-subunit in DF heterodimer in the crystal structures of A(3)B(3) and A(3)B(3)DF. In our previous study, we reported 10 mutants of E. hirae V(1)-ATPase, which showed lower binding affinities of DF with A(3)B(3) complex leading to higher initial specific ATPase activities compared to the wild-type. In this study, we identified a mutation of A-subunit (LV(476-7)AA) at its C-terminal domain resulting in the A(3)B(3) complex with higher binding affinities for wild-type or mutant DF heterodimers and lower initial ATPase activities compared to the wild-type A(3)B(3) complex, consistent with our previous proposal of reciprocal relationship between the ATPase activity and the protein-protein binding affinity of DF axis to the A(3)B(3) catalytic domain of E. hirae V-ATPase. These observations suggest that the binding of DF axis at the contact region of A(3)B(3) rotary ring is relevant to its rotation activity. Springer International Publishing 2013-12-27 /pmc/articles/PMC3879392/ /pubmed/24404436 http://dx.doi.org/10.1186/2193-1801-2-689 Text en © Alam et al.; licensee Springer. 2013 This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Alam, Jahangir Yamato, Ichiro Arai, Satoshi Saijo, Shinya Mizutani, Kenji Ishizuka-Katsura, Yoshiko Ohsawa, Noboru Terada, Takaho Shirouzu, Mikako Yokoyama, Shigeyuki Iwata, So Kakinuma, Yoshimi Murata, Takeshi Mutant LV(476-7)AA of A-subunit of Enterococcus hirae V(1)-ATPase: High affinity of A(3)B(3) complex to DF axis and low ATPase activity |
title | Mutant LV(476-7)AA of A-subunit of Enterococcus hirae V(1)-ATPase: High affinity of A(3)B(3) complex to DF axis and low ATPase activity |
title_full | Mutant LV(476-7)AA of A-subunit of Enterococcus hirae V(1)-ATPase: High affinity of A(3)B(3) complex to DF axis and low ATPase activity |
title_fullStr | Mutant LV(476-7)AA of A-subunit of Enterococcus hirae V(1)-ATPase: High affinity of A(3)B(3) complex to DF axis and low ATPase activity |
title_full_unstemmed | Mutant LV(476-7)AA of A-subunit of Enterococcus hirae V(1)-ATPase: High affinity of A(3)B(3) complex to DF axis and low ATPase activity |
title_short | Mutant LV(476-7)AA of A-subunit of Enterococcus hirae V(1)-ATPase: High affinity of A(3)B(3) complex to DF axis and low ATPase activity |
title_sort | mutant lv(476-7)aa of a-subunit of enterococcus hirae v(1)-atpase: high affinity of a(3)b(3) complex to df axis and low atpase activity |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3879392/ https://www.ncbi.nlm.nih.gov/pubmed/24404436 http://dx.doi.org/10.1186/2193-1801-2-689 |
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