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The role of I;`0 regions in protein folding David Baker, Andrew K Shiau and David A Agard
 

Summary: The role of I;`0 regions in protein folding
David Baker, Andrew K Shiau and David A Agard
University of California, San Francisco, USA
In vivo, many proteases are synthesized as larger precursors. During the
maturation process, the catalytically active protease domain is released from
the larger polypeptide or pro-enzyme by one or more proteolytic processing
steps. In several well studied cases, amino-terminal pro regions have been
shown to play a fundamental role in the folding of the associated protease
domains. The mechanism by which pro regions facilitate folding appears to
be significantly different from that used by the molecular chaperones. Recent
results suggest that the pro region assisted folding mechanism may be used
by a wide variety of proteases, and perhaps even by non-proteases.
Current Opinion in Cell Biology 1993, 5:966-970
Introduction
An increasing number of proteases have been found
to be synthesized as pro-enzymes, that is, the catalyti-
cally active protease region is eventually cleaved from
a larger precursor polypeptide. Essentially all known
extracellular bacterial proteases are made as pre-pro-
proteins (the pre region being a signal sequence),

  

Source: Agard, David - Department of Biochemistry and Biophysics, University of California at San Francisco

 

Collections: Biotechnology; Biology and Medicine