Open AccessAnionic polymers of Bacillus subtilis cell wall modulate the folding rate of secreted proteins
Author(s) -
Chambert R,
PetitGlatron M.F
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb08705.x
Subject(s) - levansucrase , bacillus subtilis , biochemistry , cell wall , secretion , chemistry , amylase , teichoic acid , biophysics , folding (dsp implementation) , calcium , kinetics , biology , enzyme , peptidoglycan , bacteria , genetics , physics , organic chemistry , quantum mechanics , electrical engineering , engineering
In order to characterize the dynamics of the interaction between the emergent membrane translocated exoprotein and the components of Bacillus subtilis cell wall, we examined the kinetics of the in vitro refolding of levansucrase and α‐amylase, at pH 7 and 37°C, in the presence of polyphosphates (polyP) of various chain lengths (2≤ n ≤65 ). These soluble anionic polymers are considered here to mimic the role of teichoic acids. Even in the absence of calcium, levansucrase rapidly refolded in the presence of polyP of n ≥16. In contrast, polyP modulate indirectly the rate of α‐amylase refolding via their affinity for calcium. These differential effects might explain that the rate of the cell wall translocation of α‐amylase secretion was found to be half that of levansucrase.