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The insect antimicrobial peptide, l ‐pyrrhocoricin, binds to and stimulates the ATPase activity of both wild‐type and lidless DnaK
Author(s) -
Chesnokova Liudmila S.,
Slepenkov Sergey V.,
Witt Stephan N.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.03.075
Subject(s) - peptide , antimicrobial , biochemistry , bacteria , atpase , chaperone (clinical) , binding site , biology , antimicrobial peptides , peptide sequence , substrate (aquarium) , enzyme , chemistry , microbiology and biotechnology , medicine , genetics , pathology , ecology , gene
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.