Iron(III) hydroxamate transport across the cytoplasmic membrane ofEscherichia coli

1991 ◽  
Vol 4 (1) ◽  
pp. 23-32 ◽  
Author(s):  
Wolfgang K�ster
Biochemistry ◽  
2005 ◽  
Vol 44 (20) ◽  
pp. 7570-7576 ◽  
Author(s):  
Jaroslaw Króliczewski ◽  
Katarzyna Hombek-Urban ◽  
Andrzej Szczepaniak

1998 ◽  
Vol 273 (27) ◽  
pp. 16897-16904 ◽  
Author(s):  
Teruo Kuroda ◽  
Naoyuki Okuda ◽  
Naoto Saitoh ◽  
Tetsuo Hiyama ◽  
Yoko Terasaki ◽  
...  

Biochemistry ◽  
2002 ◽  
Vol 41 (17) ◽  
pp. 5605-5612 ◽  
Author(s):  
Janek Kubelt ◽  
Anant K. Menon ◽  
Peter Müller ◽  
Andreas Herrmann

1993 ◽  
Vol 107 (2-3) ◽  
pp. 175-178 ◽  
Author(s):  
Dorothea Seiffer ◽  
Jürgen Robert Klein ◽  
Roland Plapp

1995 ◽  
Vol 270 (40) ◽  
pp. 23485-23490 ◽  
Author(s):  
Yoshinori Akiyama ◽  
Tohru Yoshihisa ◽  
Koreaki Ito

2001 ◽  
Vol 276 (50) ◽  
pp. 47690-47694 ◽  
Author(s):  
Makiko Terada ◽  
Toshiro Kuroda ◽  
Shin-ichi Matsuyama ◽  
Hajime Tokuda

Escherichia colilipoproteins are anchored to either the inner or outer membrane through fatty acyl chains covalently attached to an N-terminal cysteine. Aspartate at position 2 functions to retain lipoproteins in the inner membrane, although the retention is perturbed depending on the residue at position 3. We previously revealed that LolCDE and LolA play critical roles in this lipoprotein sorting. To clarify the sorting signals, the LolA-dependent release of lipoprotein derivatives having various residues at positions 2 and 3 was examined in spheroplasts. When the residue at position 3 was serine, only aspartate at position 2 caused the retention of lipoproteins in spheroplasts. We then examined the release of derivatives having aspartate at position 2 and various residues at position 3. Strong inner membrane retention occurred with a limited number of species of residues at position 3. These residues were present at position 3 of native lipoproteins having aspartate at position 2, whereas residues that inhibited the retention were not. It was also found that a strong inner membrane retention signal having residues other than aspartate at position 2 could be formed through the combination of the residues at positions 2 and 3. These results indicate that the inner membrane localization of native lipoproteins is ensured by the use of a limited number of strong inner membrane retention signals.


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