Premium
The influence of protein folding on late stages of the secretion of α‐amylases from Bacillus subtilis
Author(s) -
Stephenson Keith,
Carter Noel M,
Harwood Colin R,
Petit-Glatron Marie-Françoise,
Chambert Régis
Publication year - 1998
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/s0014-5793(98)00698-x
Subject(s) - bacillus subtilis , amylase , secretion , folding (dsp implementation) , chemistry , protein folding , biochemistry , biology , enzyme , bacteria , genetics , electrical engineering , engineering
A derivative of the α‐amylase from Bacillus licheniformis (AmyL) engineered to give an active enzyme with increased net positive charge is secreted by Bacillus subtilis with a yield that is significantly lower than that of the native enzyme. This reduction in yield is the result of increased proteolysis during or shortly after translocation through the cytoplasmic membrane. When we compared the overall rate of folding of the engineered derivative (AmyLQS50.5) with that of AmyL it exhibited a greater dependency on Ca 2+ ions for in vitro folding. When the concentration of Ca 2+ in the growth medium was increased, so too did the relative yield of AmyLQS50.5. We discuss the importance of secretory protein folding at the membrane/cell wall interface with respect to the yield of native and heterologous proteins from B. subtilis .