ABSTRACT

VS. ATP-DEPENDENT CHAPERONES SUCHIRA BOSE1, MONIKA EHRNSPERGER and JOHANNES BUCHNER*

1Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol BS8 7TD, United Kingdom

Institut für Biophysik and Physikalische Biochemie, Universität Regensburg, 93040 Regensburg, Germany

1. INTRODUCTION

Heat shock proteins (Hsps) are synthesised in response to external stresses such as a sudden increase in temperature (Nover, 1991). The predominant classes of stress proteins including GroE, Hsp70, Hsp90 and small Hsps (sHsps) have been implicated in protein folding as molecular chaperones (Morimoto et al., 1994; Jakob and Buchner, 1994; Buchner, 1996). While the precise molecular mechanisms of these chaperones are still under extensive investigation, it recently has become increasingly clear that chaperones can be divided into two groups: those that act ATP-dependently and those that function independent of ATP. Here, we will outline the properties of ATP-independent chaperones with a view to comparing their differences to ATP-dependent chaperones.