scholarly journals Primary structure of colicin M, an inhibitor of murein biosynthesis.

1987 ◽  
Vol 169 (7) ◽  
pp. 3358-3361 ◽  
Author(s):  
J Köck ◽  
T Olschläger ◽  
R M Kamp ◽  
V Braun
1982 ◽  
Vol 152 (3) ◽  
pp. 994-1000
Author(s):  
K Schaller ◽  
J V Höltje ◽  
V Braun

Colicin M inhibited the incorporation of DL + meso-2,6-diamino[3,4,5-3H]pimelic acid into the murein (peptidoglycan) of growing cells of Escherichia coli W7 dap lys. The inhibition of the UDP-N-acetylmuramyl pentapeptide-dependent incorporation of UDP-N-acetyl-D-[U-14C]glucosamine into isolated cell envelopes indicated interference with a late step of murein biosynthesis. After the inhibition of murein biosynthesis, cells lysed, and they released lysis products of murein. In vitro, the murein biosynthesis of colicin M-tolerant mutants (tolM) was inhibited by colicin M. Therefore, tolerance is probably conferred by an impaired uptake of an altered fixation close to the target site and not by a mutation of the target itself. Preliminary studies with beta-lactam antibiotics and with mutants in penicillin-binding proteins did not reveal a specific enzymatic step inhibited by colicin M. The unique action among the colicins renders colicin M a potentially useful tool for studying murein biosynthesis.


1985 ◽  
Vol 260 (4) ◽  
pp. 2301-2306
Author(s):  
H Pande ◽  
J Calaycay ◽  
D Hawke ◽  
C M Ben-Avram ◽  
J E Shively

1991 ◽  
Vol 266 (29) ◽  
pp. 19480-19483 ◽  
Author(s):  
K. Takahashi ◽  
H. Inoue ◽  
K. Sakai ◽  
T. Kohama ◽  
S. Kitahara ◽  
...  

1972 ◽  
Vol 247 (23) ◽  
pp. 7612-7621 ◽  
Author(s):  
C. Richard Savage ◽  
Tadashi Inagami ◽  
Stanley Cohen

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