Specificity of the lipase-specific foldases of gram-negative bacteria and the role of the membrane anchor |
| |
Authors: | M El Khattabi C Ockhuijsen W Bitter K-E Jaeger and J Tommassen |
| |
Institution: | (1) Department of Molecular Microbiology, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands e-mail: m.elkhattabi@bio.uu.nl Tel.: +31-30-2533119; Fax: +31-30-2513655 , NL;(2) Lehrstuhl für Biologie der Mikroorganismen, Ruhr-Universit?t, D-44780 Bochum, Germany, DE |
| |
Abstract: | Folding of lipases that are secreted by Pseudomonads and other gram-negative bacteria via the type II secretion pathway is
facilitated by dedicated chaperones, called lipase-specific foldases (Lifs). Lifs are membrane-anchored proteins with a large
periplasmic domain. The functional interaction between the Lif and its cognate lipase is specific, since the Pseudomonas aeruginosa Lif was found not to substitute for Lifs from Burkholderia glumae or Acinetobacter calcoaceticus. However, the P. aeruginosa Lif was able to activate the lipase from the closely related species P. alcaligenes. Hybrid proteins constructed from parts of the P. aeruginosa and B. glumae Lifs revealed that the C-terminal 138 amino acids of the B. glumae Lif determine the specificity of the interaction with the cognate lipase. Furthermore, the periplasmic domain of the B. glumae Lif was functional when cloned in frame with a cleavable signal sequence, which demonstrates that the membrane anchor is
not essential for Lif function in vivo. However, the recombinant Lif was released into the medium, indicating that the function
of the membrane anchor is to prevent secretion of the Lif together with the lipase.
Received: 12 November 1998 / Accepted: 19 February 1999 |
| |
Keywords: | Pseudomonas Burkholderia Lipase Foldase Secretion |
本文献已被 SpringerLink 等数据库收录! |
|