PMID:1937006
| Citation |
Anton, M and Heller, KJ (1991) Functional analysis of a C-terminally altered TonB protein of Escherichia coli. Gene 105:23-9 |
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| Abstract |
Deletions within the 3'-end of the cloned Escherichia coli tonB gene were constructed and recombined into the chromosome. Deletions affecting the last eight C-terminal amino acids (aa) yielded functionally active TonB, whereas deletion of the last 15 C-terminal aa, which removed the C-terminal hydrophobic region of TonB, abolished TonB function entirely. Distribution of TonB within cell compartments was not significantly affected by any of the deletions. All deletion derivatives were less stable than wild-type TonB. A major degradation product of approx. 29 kDa was observed for all TonB derivatives, indicating that it was an N-terminal fragment. The possibility is discussed that the C-terminal hydrophobic region is involved in the intramolecular interaction rather than in the membrane association of TonB. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacteriophages/metabolism; Base Sequence; Biological Transport/genetics; Cloning, Molecular; Colicins/pharmacology; DNA Mutational Analysis; Electrophoresis, Polyacrylamide Gel; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Ferrichrome/pharmacology; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Molecular Sequence Data; Peptide Fragments/chemistry; Peptide Fragments/genetics; Peptide Fragments/metabolism; Plasmids/genetics; Transformation, Bacterial/genetics; Vitamin B 12/pharmacology |
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