The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein. Academic Article uri icon

abstract

  • Evidence is presented that the E. coli secB gene encodes a soluble protein that interacts with the mature region of the precursor maltose-binding protein (MBP), and promotes MBP export by preventing premature folding of the newly synthesized polypeptide into an export-incompetent form. The interaction of SecB with MBP was indicated by the finding that synthesis of various export-defective MBP species interfered with normal protein export by limiting SecB availability. The antifolding activity of SecB was demonstrated by the following: the defect in MBP export in SecB- cells was suppressed by mutational alterations affecting MBP folding; export of a mutant MBP that is accomplished in a strictly posttranslational mode was totally blocked in SecB- cells; and the rate of folding of wild-type MBP synthesized in vitro was found to be accelerated when SecB was absent and greatly retarded when excess SecB was present.

published proceedings

  • Cell

author list (cited authors)

  • Collier, D. N., Bankaitis, V. A., Weiss, J. B., & Bassford, P. J.

citation count

  • 304

complete list of authors

  • Collier, DN||Bankaitis, VA||Weiss, JB||Bassford, PJ

publication date

  • April 1988

published in