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2017 ; 7
(ä): 44324
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Antimicrobial peptide gramicidin S is accumulated in granules of producer cells
for storage of bacterial phosphagens
#MMPMID28295017
Berditsch M
; Trapp M
; Afonin S
; Weber C
; Misiewicz J
; Turkson J
; Ulrich AS
Sci Rep
2017[Mar]; 7
(ä): 44324
PMID28295017
show ga
Many antimicrobial peptides are synthesized non-ribosomally in bacteria, but
little is known about their subcellular route of biosynthesis, their mode of
intracellular accumulation, or their role in the physiology of the producer
cells. Here, we present a comprehensive view on the biosynthesis of gramicidin S
(GS) in Aneurinibacillus migulanus, having observed a peripheral membrane
localization of its synthetases. The peptide gets accumulated in nano-globules,
which mature by fusion into larger granules and end up within vacuolar
structures. These granules serve as energy storage devices, as they contain GS
molecules that are non-covalently attached to alkyl phosphates and protect them
from dephosphorylation and premature release of energy. This finding of a
fundamentally new type of high-energy phosphate storage mechanism can explain the
curious role of GS biosynthesis in the physiology of the bacterial producer
cells. The unknown role of the GrsT protein, which is part of the non-ribosomal
GS synthetase operon, can thus be assumed to be responsible for the biosynthesis
of alkyl phosphates. GS binding to alkyl phosphates may suggest its general
affinity to phosphagens such as ATP and GTP, which can represent the important
intracellular targets in pathogenic bacteria.