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A newly isolated Pex7-binding, atypical PTS2 protein P7BP2 is a novel dynein-type AAA+ protein.
Niwa, Hajime; Miyauchi-Nanri, Yasuhiro; Okumoto, Kanji; Mukai, Satoru; Noi, Kentaro; Ogura, Teru; Fujiki, Yukio.
Affiliation
  • Niwa H; Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, Japan.
  • Miyauchi-Nanri Y; Department of Biology, Faculty of Sciences, Kyushu University, 744 Motooka Nishi-ku, Fukuoka, Japan.
  • Okumoto K; Department of Biology, Faculty of Sciences, Kyushu University, 744 Motooka Nishi-ku, Fukuoka, Japan.
  • Mukai S; Department of Biology, Faculty of Sciences, Kyushu University, 744 Motooka Nishi-ku, Fukuoka, Japan.
  • Noi K; Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, Japan.
  • Ogura T; Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Saitama, Japan.
  • Fujiki Y; Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, Japan.
J Biochem ; 164(6): 437-447, 2018 Dec 01.
Article in En | MEDLINE | ID: mdl-30204880
ABSTRACT
A newly isolated binding protein of peroxisomal targeting signal type 2 (PTS2) receptor Pex7, termed P7BP2, is transported into peroxisomes by binding to the longer isoform of Pex5p, Pex5pL, via Pex7p. The binding to Pex7p and peroxisomal localization of P7BP2 depends on the cleavable PTS2 in the N-terminal region, suggesting that P7BP2 is a new PTS2 protein. By search on human database, three AAA+ domains are found in the N-terminal half of P7BP2. Protein sequence alignment and motif search reveal that in the C-terminal region P7BP2 contains additional structural domains featuring weak but sufficient homology to AAA+ domain. P7BP2 behaves as a monomer in gel-filtration chromatography and the single molecule observed under atomic force microscope shapes a disc-like ring. Collectively, these results suggest that P7BP2 is a novel dynein-type AAA+ family protein, of which domains are arranged into a pseudo-hexameric ring structure.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Adenosine Triphosphatases / Peroxisomes / Peroxisomal Targeting Signal 2 Receptor / Peroxisome-Targeting Signal 1 Receptor Limits: Animals / Humans Language: En Journal: J Biochem Year: 2018 Document type: Article Affiliation country: Japón

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Adenosine Triphosphatases / Peroxisomes / Peroxisomal Targeting Signal 2 Receptor / Peroxisome-Targeting Signal 1 Receptor Limits: Animals / Humans Language: En Journal: J Biochem Year: 2018 Document type: Article Affiliation country: Japón