tailieunhanh - Báo cáo khoa học: Structural and functional analysis of the interaction of the AAA-peroxins Pex1p and Pex6p

The AAA-peroxins Pex1p and Pex6p play a critical role in peroxisome bio-genesis but their precise function remains to be established. These two peroxins consist of three distinct regions (N, D1, D2), two of which (D1, D2) contain a conserved 230 amino acid cassette, which is common to all ATPases associated with various cellular activities (AAA). Here we show that Pex1p and Pex6p from Saccharomyces cerevisiaedo interact in vivo. We assigned their corresponding binding sites and elucidated the importance of ATP-binding and -hydrolysis of Pex1p and Pex6p for their interaction. . | ềFEBS Journal Structural and functional analysis of the interaction of the AAA-peroxins Pexlp and Pex6p Ingvild Birschmann1 f Katja Rosenkranz2 f Ralf Erdmann2 and Wolf-H Kunau1 1 Abteilung fur Zellbiochemie Medizinische Fakultat der Ruhr-Universitat Bochum Germany 2 Abteilung fur Systembiochemie Medizinische Fakultat der Ruhr-Universitat Bochum Germany Keywords AAA-proteins peroxisomalbiogenesis Pexlp Pex6p peroxin Correspondence Dr Ralf Erdmann Institut fur Physiologische Chemie Abteilung fuur Systembiochemie Medizinische Fakultat der Ruhr-Universitat Bochum D-44780 Bochum Germany. Tel 49 234322 4943 Fax 49 234321 4266 E-mail Present address Institut fuur Klinische Biochemie und Patho-biochemie Medizinische Universitatsklinik D-97078 Wurzburg Germany The AAA-peroxins Pexlp and Pex6p play a critical role in peroxisome biogenesis but their precise function remains to be established. These two peroxins consist of three distinct regions N D1 D2 two of which D1 D2 contain a conserved w 230 amino acid cassette which is common to all ATPases associated with various cellular activities AAA . Here we show that Pex1p and Pex6p from Saccharomyces cerevisiae do interact in vivo. We assigned their corresponding binding sites and elucidated the importance of ATP-binding and -hydrolysis of Pex1p and Pex6p for their interaction. We show that the interaction of Pex1p and Pex6p involves their first AAA-cassettes and demonstrate that ATP-binding but not ATP-hydrolysis in the second AAA-cassette D2 of Pex1p is required for the Pex1p-Pex6p interaction. Furthermore we could prove that the second AAA-cassettes D2 of both Pex1p and Pex6p were essential for peroxisomal biogenesis and thus probably comprise the overall activity of the proteins. fBoth authors contributed equally to this manuscript Received 21 July 2004 accepted 25 August 2004 doi Peroxisomes are ubiquitous single membrane-bound organelles involved in many .

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