tonB-independent ferrichrome-mediated iron transport in Escherichia coli spheroplasts.
نویسندگان
چکیده
Although a functional tonB gene product was required for ferrichrome-mediated iron transport in whole cells of Escherichia coli K-12, such transport did not require the tonB+ function in spheroplasts. We suggest that in spheroplasts ferrichrome has direct access to the cytoplasmic membrane and that this is reflected in tonB-independent accumulation of ferrichrome iron. Therefore, the tonB gene product does not function in the translocation of ferrichrome iron across the inner membrane.
منابع مشابه
Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide.
FhuA, the receptor for ferrichrome-iron in Escherichia coli, is a member of a family of integral outer membrane proteins, which, together with the energy-transducing protein TonB, mediate the active transport of ferric siderophores across the outer membrane of Gram-negative bacteria. The three-dimensional structure of FhuA is presented here in two conformations: with and without ferrichrome-iro...
متن کاملIron transport in Escherichia coli: uptake and modification of ferrichrome.
During the transport of iron as ferrichrome complex into cells of Escherichia coli K-12, the ligand was modified and excreted into the medium. The rate of the formation of the modified product corresponded with the rate of iron transport. The modified product showed a decreased affinity for ferric iron and did not serve as an effective iron ionophore. After all of the ferrichrome had been conve...
متن کاملIn vivo synthesis of the periplasmic domain of TonB inhibits transport through the FecA and FhuA iron siderophore transporters of Escherichia coli.
The siderophore transport activities of the two outer membrane proteins FhuA and FecA of Escherichia coli require the proton motive force of the cytoplasmic membrane. The energy of the proton motive force is postulated to be transduced to the transport proteins by a protein complex that consists of the TonB, ExbB, and ExbD proteins. In the present study, TonB fragments lacking the cytoplasmic m...
متن کاملLoop deletions indicate regions important for FhuA transport and receptor functions in Escherichia coli.
Precise deletions of cell surface-exposed loops of FhuA resulted in mutants of Escherichia coli with distinct phenotypes. Deletion of loop 3 or 11 inactivated ferrichrome transport activity. Deletion of loop 8 inactivated receptor activity for colicin M and the phages T1, T5, and phi80. The loop 7 deletion mutant was colicin M resistant but fully phage sensitive. The loop 4 deletion mutant was ...
متن کاملBinding of iron-free siderophore, a common feature of siderophore outer membrane transporters of Escherichia coli and Pseudomonas aeruginosa.
TonB-dependent iron transporters present in the outer membranes of Gram-negative bacteria transport ferric-siderophore complexes into the periplasm. This requires proton motive force and an integral inner membrane complex, TonB-ExbB-ExbD. Recognition of iron-free siderophores by TonB-dependent outer membrane transporters (OMT) has only been described for a subfamily called OMT(N). These OMT(N)s...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of bacteriology
دوره 143 3 شماره
صفحات -
تاریخ انتشار 1980