Naoki Ichikawa

Summary

Affiliation: Osaka City University
Country: Japan

Publications

  1. Ichikawa N, Chisuwa N, Tanase M, Nakamura M. Mitochondrial ATP synthase residue betaarginine-408, which interacts with the inhibitory site of regulatory protein IF1, is essential for the function of the enzyme. J Biochem. 2005;138:201-7 pubmed
  2. Ichikawa N, Karaki A, Kawabata M, Ushida S, Mizushima M, Hashimoto T. The region from phenylalanine-17 to phenylalanine-28 of a yeast mitochondrial ATPase inhibitor is essential for its ATPase inhibitory activity. J Biochem. 2001;130:687-93 pubmed
    ..These results show that the region from the position 17 to 28 of the yeast inhibitor is the most important for its activity and is required for the inhibition of F(1), rather than binding to the enzyme. ..
  3. Ichikawa N, Nakabayashi K, Hashimoto T. A yeast mitochondrial ATPase inhibitor interacts with three proteins that are easy to dissociate from the mitochondrial inner membrane. J Biochem. 2002;132:649-54 pubmed
    ..These results shows that the endogenous inhibitor binds not only to the catalytic part of the enzyme, but also to the 19-21 kDa proteins that loosely associate with the mitochondrial inner membrane. ..
  4. Ichikawa N, Ogura C. Overexpression, purification, and characterization of human and bovine mitochondrial ATPase inhibitors: comparison of the properties of mammalian and yeast ATPase inhibitors. J Bioenerg Biomembr. 2003;35:399-407 pubmed
    ..Common inhibitory sites of mammalian and yeast inhibitors are suggested. ..
  5. Sun L, Nakamae N, Ichikawa N. The region from phenylalanine-28 to lysine-50 of a yeast mitochondrial ATPase inhibitor (IF1) forms an α-helix in solution. J Bioenerg Biomembr. 2015;47:457-65 pubmed publisher
    ..The results suggest that the helix of yeast IF1 facilitates binding to F(1) by promoting initial interaction of the proteins. ..
  6. Ichikawa N, Ushida S, Kawabata M, Masazumi Y. Nucleotide sequence of cDNA coding the mitochondrial precursor protein of the ATPase inhibitor from humans. Biosci Biotechnol Biochem. 1999;63:2225-7 pubmed
    ..The deduced protein sequence shows that the protein was composed of 106 amino acids and had a molecular weight of 12248. The structural features of the protein show that the cDNA isolated in this study codes the human ATPase inhibitor. ..
  7. Ichikawa N, Mizuno M. Functional expression of hexahistidine-tagged beta-subunit of yeast F1-ATPase and isolation of the enzyme by immobilized metal affinity chromatography. Protein Expr Purif. 2004;37:97-101 pubmed
    ..The application of this novel procedure simplifies the number of steps required for the isolation of F1 used for studying the molecular mechanism of catalysis and regulation of the enzyme. ..
  8. Ichikawa N, Ando C, Fumino M. Caenorhabditis elegans MAI-1 protein, which is similar to mitochondrial ATPase inhibitor (IF1), can inhibit yeast F0F1-ATPase but cannot be transported to yeast mitochondria. J Bioenerg Biomembr. 2006;38:93-9 pubmed
    ..MAI-2-GFP fusion protein was transported to yeast mitochondria, but MAI-1-GFP was not. These results indicate that the MAI-2 is (C. elegans) IF(1). MAI-1 seems to be a cytosolic protein and may regulate cytosolic ATPase(s). ..