Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 68, 2004 - Issue 2
Journal homepage
125
Views
5
CrossRef citations to date
0
Altmetric
Original Articles

Identification of Nucleotide Binding Sites in V-Type Na+-ATPase from Enterococcus hirae

Toshiaki HOSAKADepartment of Biological Science and Technology, Tokyo University of Science
,
Takeshi MURATAThe Medical Research Council Dunn Human Nutrition Unit
,
Yoshimi KAKINUMADepartment of Applied Chemistry, Muroran Institute of Technology
&
Ichiro YAMATODepartment of Biological Science and Technology, Tokyo University of Science
Pages 293-299 | Received 30 Jun 2003, Accepted 14 Oct 2003, Published online: 22 May 2014

  • 1) Senior, A. E., The proton-translocating ATPase of Escherichia coli. Ann. Rev. Biopys. Chem., 19, 7–41 (1990).
  • 2) Nelson, N., and Taiz, L., The evolution of H+-ATPases. Trends Biochem. Sci., 14, 113–116 (1989).
  • 3) Gogarten, J. P., Kibak, H., Dittrich, P., Taiz, L., Bowman, E. J., Bowman, B. J., Manolson, M. F., Poole, R. J., Data, T., Oshima, T., Konishi, J., Denda, K., and Yoshida, M., Evolution of the vacuolar H+-ATPase: implications for the origin of eukaryotes. Proc. Natl. Acad. Sci. USA, 86, 6661–6665 (1989).
  • 4) Futai, M., Noumi, T., and Maeda, M., ATP synthase (H+-ATPase): Results by combined biochemical and molecular biological approaches. Ann. Rev. Biochem., 58, 111–136 (1989).
  • 5) Stevens, T. H., and Forgac, M., Structure, function and regulation of the vacuolar (H+)-ATPase. Annu. Rev. Cell Dev. Biol., 13, 779–808 (1997).
  • 6) Abrahams, J. P., Leslie, A. G. W., Lutter, R., and Walker, J. E., Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature, 370, 621–628 (1994).
  • 7) Noji, H., Yasuda, R., Yoshida, M., and Kinosita, K. Jr., Direct observation of the rotation of F1-ATPase. Nature, 386, 299–302 (1997).
  • 8) Imamura, H., Nakano, M., Noji, H., Muneyuki, E., Ohkuma, S., Yoshida, M., and Yokoyama, K., Evidence for rotation of V1-ATPase. Proc. Natl. Acad. Sci. USA, 100, 2312–2315 (2003).
  • 9) Dimroth, P., Wang, H., Grabe, M., and Oster, G., Energy transduction in the sodium F-ATPase of Propionigenium modestum. Proc. Natl. Acad. Sci. USA, 96, 4924–4929 (1999).
  • 10) Murata, T., Yoshikawa, Y., Toshiaki, H., Takase, K., Kakinuma, Y., Yamato, I., and Kikuchi, T., Nucleotide binding sites in V-type Na+-ATPase from Enterococcus hirae. J. Biochem., 132, 789–794 (2002).
  • 11) Takase, K., Yamato, I., and Kakinuma, Y., Cloning and sequencing of the genes coding for the A and B subunits of vacuolar-type Na+-ATPase from Enterococcus hirae. J. Biol. Chem., 268, 11610–11616 (1993).
  • 12) Shao, E., Nishi, T., Kawasaki-Nishi, S., and Forgac, M., Mutational analysis of the non-homologous region of subunit A of the yeast V-ATPase. J. Biol. Chem., 278, 12985–12991 (2003).
  • 13) Vasilyeva, E., Liu, Q., Macleod, K. J., Baleja, J. D., and Forgac, M., Cysteine-scanning mutagenesis of the noncatalytic nucleotide binding site of the Yeast V-ATPase. J. Biol. Chem., 275, 255–260 (2000).
  • 14) Takase, K., Kakinuma, S., Yamato, I., Konishi, K., Igarashi, K., and Kakinuma, Y., Sequencing and characterization of the ntp gene cluster for vacuolar-type Na+-translocating ATPase of Enterococcus hirae. J. Biol. Chem., 269, 11037–11044 (1994).
  • 15) Murata, T., Takase, K., Yamato, I., Igarashi, K., and Kakinuma, Y., Purification and reconstitution of Na+-translocating vacuolar ATPase from Enterococcus hirae. J. Biol. Chem., 272, 24885–24890 (1997).
  • 16) Murata, T., Takase, K., Yamato, I., Igarashi, K., and Kakinuma, Y., Properties of the V0V1 Na+-ATPase from Enterococcus hirae and its V0 moiety. J. Biochem. (Tokyo), 272, 24885–24890 (1999).
  • 17) Kakinuma, Y., and Igarashi, K., Purification and characterization of the catalytic moiety of vacuolar-type Na+-ATPase from Enterococcus hirae. J. Biochem., 116, 1302–1308 (1994).
  • 18) Murata, T., Igarashi, K., Kakinuma, Y., and Yamato, I., Na+ binding of V-type Na+-ATPase in Enterococcus hirae. J. Biol. Chem., 275, 13415–13419 (2000).
  • 19) Murata, T., Kakinuma, Y., and Yamato, I., ATP-dependent affinity change of Na+ binding sites of V-ATPase in Enterococcus hirae. J. Biol. Chem., 276, 48337–48340 (2001).
  • 20) Futai, M., Iwamoto, A., Omote, H., and Maeda, M., A glycine-rich sequence in the catalytic site of F-type ATPase. J. Bioenerg. Biomembr., 24, 463–467 (1992).
  • 21) Pedersen, P. L., and Amzel, L. M., ATP synthases. Structure, reaction center, mechanism, and regulation of one of nature’s most unique machines. J. Biol. Chem., 268, 9937–9940 (1993).
  • 22) Penefsky, H. S., and Cross, R. L., Structure and mechanism of FoF1-type ATP synthases and ATPases. Adv. Enzymol., 64, 173–214 (1991).
  • 23) Yokoyama, K., Muneyuki, E., Amano, T., Mizutani, S., Yoshida, M., Ishida, M., and Ohkuma, S., V-ATPase of Thermus thermophilus is inactivated during ATP hydrolysis but can synthesize ATP. J. Biol. Chem., 273, 20504–20510 (1998).
  • 24) Vasilyeva, E., and Forgac, M., 3′-O-(4-Benzoyl)benzoyladenosine 5′-triphosphate inhibits activity of the vacuolar H+ATPase from bovine brain clathrin-coated vesicles by modification of a rapidly exchangeable, noncatalytic nucleotide binding site on the B subunit. J. Biol. Chem., 271, 12775–12782 (1996).
  • 25) Zhang, J., Vasilyeva, E., Feng, Y., and Forgac, M., Inhibition and labeling of the coated vesicle V-ATPase by 2-azido-[32P]ATP. J. Biol. Chem., 270, 15494–15500 (1995).
  • 26) Peng, S.-B., Nucleotide labeling and reconstitution of the recombinant 58-kDa subunit of the vacuolar proton-translocating ATPase. J. Biol. Chem., 270, 16926–16931 (1995).
  • 27) Berggren, K., Chernokalskaya, E., Steinberg, T. H., Kemper, C., Lopez, M. F., Diwu, Z., Haugland, R. P., and Patton, W. F., Background-free, high sensitivity staining of proteins in one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gels using a luminescent ruthenium complex. Electrophoresis, 21, 2509–2521 (2000).
  • 28) Takase, K., Yamato, I., Igarashi, K., and Kakinuma, Y., Indispensable glutamic acid residue-139 of NtpK proteolipid in the reaction of vacuolar Na+-translocating ATPase in Enterococcus hirae. Biosci. Biotechnol. Biochem., 63, 1125–1129 (1999).
  • 29) Schagger, H., and von Jagow, G., Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368–379 (1987).
  • 30) Cross, R. L., Cunningham, D., Miller, C. G., Xue, Z. X., Zhou, J. M., and Boyer, P. D., Adenine nucleotide binding sites on beef heart F1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site. Proc. Natl. Acad. Sci. USA, 84, 5715–5719 (1987).
  • 31) Wise, J. G., Hicke, B. J., and Boyer, P. D., Catalytic and noncatalytic nucleotide binding sites of the Escherichia coli F1 ATPase. Amino acid sequences of beta-subunit tryptic peptides labeled with 2-azido-ATP. FEBS Lett., 223, 395–401 (1987).
  • 32) Weber, J., Wilke-Mounts, S., Lee, R. S., Grell, E., and Senior, A. E., Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied. J. Biol. Chem., 268, 6241–6247 (1993).
  • 33) MacLeod, K. J., Vasilyeva, E., Merdek, K., Vogel, P. D., and Forgac, M., Photoaffinity labeling of wild-type and mutant forms of the yeast V-ATPase A subunit by 2-azido-[32P]ADP. J. Biol. Chem., 274, 32869–32874 (1999).
  • 34) Bullough, D. A., and Allison, W. S., Inactivation of the bovine heart mitochondrial F1-ATPase by 5′-p-fluorosulfonylbenzoyl[3H]inosine is accompanied by modification of tyrosine 345 in a single beta subunit. J. Biol. Chem., 261, 14171–14177 (1986).
  • 35) Liu, Q., Kane, P. M., Newman, P. R., and Forgac, M., Site-directed mutagenesis of the yeast V-ATPase B subunit (Vma2p). J. Biol. Chem., 271, 2018–2022 (1996).
  • 36) Weber, J., Lee, R. S., Wilke-Mounts, S., Grell, E., and Senior, A. E., Combined application of site-directed mutagenesis, 2-azido-ATP labeling, and lin-benzo-ATP binding to study the noncatalytic sites of Escherichia coli F1-ATPase. J. Biol. Chem., 268, 6241–6247 (1993).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.