Heat shock proteins induce pores in membranes.

G M Alder, B M Austen, C L Bashford, A Mehlert, C A Pasternak
Author Information
  1. G M Alder: Department of Cellular and Molecular Sciences, St George's Hospital Medical School, London.

Abstract

Human heat shock protein (hsp) 70 and bacterial protein groEL promote leakage of calcein from liposomes induced by human serum albumin signal peptide, by S. aureus alpha toxin or by diphtheria toxin. Hsp 70 and groEL, as well as two mycobacterial homologues hsp 71 and hsp 65, induce ion conducting pores across planar lipid bilayers at low or neutral pH. It is concluded that hsp induce pores in membranes and that this may contribute to their action within cells.

MeSH Term

Amino Acid Sequence
Bacterial Proteins
Cell Membrane Permeability
Chaperonin 60
Drug Synergism
Fluoresceins
Heat-Shock Proteins
Hydrogen-Ion Concentration
Ion Channel Gating
Liposomes
Molecular Sequence Data
Protein Sorting Signals
Type C Phospholipases

Chemicals

Bacterial Proteins
Chaperonin 60
Fluoresceins
Heat-Shock Proteins
Liposomes
Protein Sorting Signals
Type C Phospholipases
fluorexon

Word Cloud

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