The influence of protein folding on late stages of the secretion of α‐amylases from Bacillus subtilis

FEBS Letters

Harwood, Colin R¹  Stephenson, Keith¹  Petit-Glatron, Marie-Françoise²  Carter, Noel M¹  Chambert, Régis² 

[1] School of Microbiological, Immunological and Virological Sciences, The Medical School, University of Newcastle upon Tyne, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK;Institut Jacques Monod, CNRS, Université Paris 6 - Paris 7, Laboratoire Genétiqué et Membranes, Tour 43-2, Place Jussieu, 75251 Paris Cedex 05, France

关键词: Protein secretion;    Folding;    Cell wall;    Calcium ion;   

DOI  :  10.1016/S0014-5793(98)00698-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Ca²⁺ ions for in vitro folding. When the concentration of Ca²⁺ 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.

【 授权许可】

Unknown