Folding in vitro and transport in vivo of pre-p-lactamase are SecB independent.

Autor: Laminet, A. A., Kumamoto, C. A., Plückthun, A.
Předmět:
Zdroj: Molecular Microbiology; Jan1991, Vol. 5 Issue 1, p117-122, 6p, 1 Diagram, 2 Charts, 1 Graph
Abstrakt: The rate of folding of the precursor of β-lactamase is not influenced by the presence of SecB under conditions in which GroEL/ES retards the folding. Wild-type (β-lactamase and several mutants in the signal or the mature protein, affecting either transport or enzyme kinetics and probably folding, were examined for total expression, total enzymatic activity, and transported β-lactamase (in vivo resistance) in secB and secB+ strains. We conclude that there is no indication of any relevant interaction between SecB- and pre-p-lactamase in vitro, nor did the secB+ mutation affect the transport of wild-type β-lactamase or any of the mutants in vivo. Thus, putative Escherichia coli 'folding modulators' must be of limited specificity. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index