| Autor: |
Chesnokova, Liudmila S., Slepenkov, Sergey V., Witt, Stephan N. |
| Předmět: |
|
| Zdroj: |
FEBS Letters; May2004, Vol. 565 Issue 1-3, p65-69, 5p |
| Abstrakt: |
Recent reports have indicated that insect antimicrobial peptides kill bacteria by inhibiting the molecular chaperone DnaK. It was proposed that the antimicrobial peptide, all-l-pyrrhocoricin (l-PYR), binds to two sites on DnaK, the conventional substrate-binding site and the multi-helical C-terminal lid, and that inhibition of DnaK comes about from the lid mode of binding. In this report, we show using two different assays that l-PYR binds to and stimulates the ATPase activity of both wild-type and a lidless variant of DnaK. Our study shows that l-PYR interacts with DnaK much like the all-l NR (NRLLLTG) peptide, which is known to bind in the conventional substrate-binding site of DnaK. l-PYR antimicrobial activity is thus a consequence of the competitive inhibition of bacterial DnaK. [Copyright &y& Elsevier] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
Plný text