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Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis.

In English

Författare

  • Marika Vitikainen
  • Ilkka Lappalainen
  • Raili Seppala
  • Haike Antelmann
  • Harry Boer
  • Suvi Taira
  • Harri Savilahti
  • Michael Hecker
  • Mauno Vihinen
  • Matti Sarvas
  • Vesa P Kontinen
Visa allt

Summary, in English

The PrsA protein of Bacillus subtilis is an essential membrane-bound lipoprotein that is assumed to assist post-translocational folding of exported proteins and stabilize them in the compartment between the cytoplasmic membrane and cell wall. This folding activity is consistent with the homology of a segment of PrsA with parvulin-type peptidyl-prolyl cis/trans isomerases (PPIase). In this study, molecular modeling showed that the parvulin-like region can adopt a parvulin-type fold with structurally conserved active site residues. PrsA exhibits PPIase activity in a manner dependent on the parvulin-like domain. We constructed deletion, peptide insertion, and amino acid substitution mutations and demonstrated that the parvulin-like domain as well as flanking N- and C-terminal domains are essential for in vivo PrsA function in protein secretion and growth. Surprisingly, none of the predicted active site residues of the parvulin-like domain was essential for growth and protein secretion, although several active site mutations reduced or abolished the PPIase activity or the ability of PrsA to catalyze proline-limited protein folding in vitro. Our results indicate that PrsA is a PPIase, but the essential role in vivo seems to depend on some non-PPIase activity of both the parvulin-like and flanking domains.

Publiceringsår

2004

Språk

Engelska

Sidor

19302-19314

Publikation/Tidskrift/Serie

Journal of Biological Chemistry

Volym

279

Issue

18

Dokumenttyp

Artikel i tidskrift

Förlag

American Society for Biochemistry and Molecular Biology

Ämne

  • Medical Genetics

Nyckelord

  • Bacillus subtilis: chemistry
  • Bacillus subtilis: metabolism
  • Bacterial Proteins: chemistry
  • Lipoproteins: chemistry
  • Lipoproteins: genetics
  • Lipoproteins: physiology
  • Membrane Proteins: chemistry
  • Membrane Proteins: genetics
  • Membrane Proteins: physiology
  • Peptidylprolyl Isomerase: chemistry
  • Proteins: secretion

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 1083-351X