The 70-kDa Peroxisomal Membrane Protein (PMP70), an ATP-Binding Cassette Transporter

2000 ◽  
Vol 32 (1-3) ◽  
pp. 131-138 ◽  
Author(s):  
Tsuneo Imanaka ◽  
Kazutoshi Aihara ◽  
Yasuyuki Suzuki ◽  
Sadaki Yokota ◽  
Takashi Osumi
1999 ◽  
Vol 274 (17) ◽  
pp. 11968-11976 ◽  
Author(s):  
Tsuneo Imanaka ◽  
Kazutoshi Aihara ◽  
Tatsuya Takano ◽  
Atsushi Yamashita ◽  
Ryuichiro Sato ◽  
...  

2013 ◽  
Vol 394 (11) ◽  
pp. 1371-1384 ◽  
Author(s):  
Michael H.H. Lenders ◽  
Sven Reimann ◽  
Sander H. J. Smits ◽  
Lutz Schmitt

Abstract Type 1 secretion systems are one of the main machineries in Gram-negative bacteria involved in the secretion of a wide range of substrates from the cytoplasm across the inner and outer membrane in one step to the extracellular space. The range of substrates varies from small proteins up to large surface layer proteins of about 900 kDa. Most of the substrates have a non-cleavable C-terminal secretion signal and so-called GG repeats that are able to bind calcium ions. The translocator complex is composed of a trimeric outer membrane protein that provides a pore in the outer membrane. A multimeric membrane fusion protein spans the periplasm and forms a continuous channel connecting the outer membrane protein with a dimeric ATP-binding cassette transporter in the inner membrane. The ATP-binding cassette-transporter is thought to form a channel through the inner membrane and energizes the transport process. This review will provide a detailed view of the components of the translocator and will summarize structural as well as functional data.


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