Biogenesis of β-barrel membrane proteins of mitochondria

被引:115
作者
Paschen, SA [1 ]
Neupert, W [1 ]
Rapaport, D [1 ]
机构
[1] Univ Munich, Inst Physiol Chem, D-81377 Munich, Germany
关键词
D O I
10.1016/j.tibs.2005.08.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
beta-Barrel membrane proteins have several important functions in outer membranes of Gram-negative bacteria and in the organelles of endosymbiotic origin, mitochondria and chloroplasts. The biogenesis of beta-barrel membrane proteins was, until recently, an unresolved process. A breakthrough was achieved when a specific pathway for the insertion of beta-barrel outer-membrane proteins was identified in both mitochondria and Gram-negative bacteria. The key component of this pathway is Tob55 (also known as Sam50) in mitochondria and Omp85 in bacteria, both beta-barrel membrane proteins themselves. Tob55 is part of the hetero-oligomeric TOB (topogenesis of mitochondrial outer-membrane beta-barrel proteins) or SAM (sorting and assembly of mitochondria) complex, which is present in the mitochondrial outer membrane. Tob55 belongs to an evolutionarily conserved protein family, the members of which are present in almost all eukaryotes and in Gram-negative bacteria and chloroplasts. Thus, is it emphasized that the insertion pathway of mitochondrial beta-barrel membrane proteins was conserved during evolution of mitochondria from endosymbiotic bacterial ancestors.
引用
收藏
页码:575 / 582
页数:8
相关论文
共 66 条
[1]   Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria [J].
Ahting, U ;
Thieffry, M ;
Engelhardt, H ;
Hegerl, R ;
Neupert, W ;
Nussberger, S .
JOURNAL OF CELL BIOLOGY, 2001, 153 (06) :1151-1160
[2]   Metaxin is a component of a preprotein import complex in the outer membrane of the mammalian mitochondrion [J].
Armstrong, LC ;
Komiya, T ;
Bergman, BE ;
Mihara, K ;
Bornstein, P .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (10) :6510-6518
[3]   A YEAST MITOCHONDRIAL OUTER-MEMBRANE PROTEIN ESSENTIAL FOR PROTEIN IMPORT AND CELL VIABILITY [J].
BAKER, KP ;
SCHANIEL, A ;
VESTWEBER, D ;
SCHATZ, G .
NATURE, 1990, 348 (6302) :605-609
[4]   Origami in the outer membrane: the transmembrane arrangement of mitochondrial porins [J].
Bay, DC ;
Court, DA .
BIOCHEMISTRY AND CELL BIOLOGY, 2002, 80 (05) :551-562
[5]   A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to cytoskeleton-based segregation machinery [J].
Boldogh, IR ;
Nowakowski, DW ;
Yang, HC ;
Chung, HS ;
Karmon, S ;
Royes, P ;
Pon, LA .
MOLECULAR BIOLOGY OF THE CELL, 2003, 14 (11) :4618-4627
[6]   Biogenesis of the gram-negative bacterial outer membrane [J].
Bos, MP ;
Tommassen, J .
CURRENT OPINION IN MICROBIOLOGY, 2004, 7 (06) :610-616
[7]   Membrane proteins: A new method enters the fold [J].
Bowie, JU .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (12) :3995-3996
[8]   Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant [J].
Doerrler, WT ;
Raetz, CRH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (30) :27679-27687
[9]   A Toc75-like protein import channel is abundant in chloroplasts [J].
Eckart, K ;
Eichacker, L ;
Sohrt, K ;
Schleiff, E ;
Heins, L ;
Soll, J .
EMBO REPORTS, 2002, 3 (06) :557-562
[10]   Protein folding: Importance of the Anfinsen cage [J].
Ellis, RJ .
CURRENT BIOLOGY, 2003, 13 (22) :R881-R883