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PEX1 is a type II AAA-ATPase that is indispensable for biogenesis and maintenance of the peroxisome, an organelle responsible for the primary metabolism of lipids, such asb-oxidation and lipid biosynthesis. Recently, we demonstrated a striking structural similarity between its N-terminal domain and those of other membrane-related AAA-ATPases, such as valo-sin-containing protein (p97). | ỊFEBS Journal The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP p97 Kumiko Shiozawa1 Natsuko Goda1 Toshiyuki Shimizu1 Kenji Mizuguchi2 3 Naomi Kondo4 Nobuyuki Shimozawa4 5 Masahiro Shirakawa1 6 and Hidekazu Hiroaki1 1 InternationalGraduate Schoolof Arts and Sciences Yokohama City University Tsurumi-ku Yokohama Kanagawa Japan 2 Department of Biochemistry University of Cambridge UK 3 Department of Applied Mathematics and TheoreticalPhysics Centre for MathematicalSciences University of Cambridge UK 4 Department of Pediatrics Gifu University Schoolof Medicine Japan 5 Division of Genomic Research Life Science Research Center Gifu University Japan 6 Department of Molecular Engineering Graduate Schoolof Engineering Kyoto University Japan Keywords AAA-ATPase N-terminaldomain PEX1 phospholipid valosine-containing protein Correspondence H. Hiroaki Division of Molecular Biophysics Graduate School of Integrated Sciences Yokohama City University 1-7-29 Suehirocho Tsurumi Yokohama Kanagawa Japan 230-0045 Fax 81 45 508 7361 Tel 81 45 508 7214 E-mail hiroakih@tsurumi.yokohama-cu.ac.jp Received 21 June 2006 revised 6 September 2006 accepted 11 september 2006 doi 10.1111 j.1742-4658.2006.05494.x PEX1 is a type II AAA-ATPase that is indispensable for biogenesis and maintenance of the peroxisome an organelle responsible for the primary metabolism of lipids such as b-oxidation and lipid biosynthesis. Recently we demonstrated a striking structural similarity between its N-terminal domain and those of other membrane-related AAA-ATPases such as valo-sin-containing protein p97 . The N-terminal domain of valosine-containing protein serves as an interface to its adaptor proteins p47 and Ufd1 whereas the physiologic interaction partner of the N-terminal domain of PEX1 remains unknown. Here we found that N-terminal domains isolated from valosine-containing protein as well as from PEX1 bind phosphoinositides. The N-terminal domain of PEX1 appears to .
