The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity.

Abstract:

:Selective protein degradation is an energy-dependent process performed by high-molecular-weight proteases. The activity of proteolytic components of these enzymes is coupled to the ATPase activity of their regulatory subunits or domains. Here, we obtained the proteolytic domain of Escherichia coli protease Lon by cloning the corresponding fragment of the lon gene in pGEX-KG, expression of the hybrid protein, and isolation of the proteolytic domain after hydrolysis of the hybrid protein with thrombin. The isolated proteolytic domain exhibited almost no activity toward protein substrates (casein) but hydrolyzed peptide substrates (melittin), thereby confirming the importance of the ATPase component for protein hydrolysis. Protease Lon and its proteolytic domain differed in the efficiency and specificity of melittin hydrolysis.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Rasulova FS,Dergousova NI,Starkova NN,Melnikov EE,Rumsh LD,Ginodman LM,Rotanova TV

doi

10.1016/s0014-5793(98)00859-x

subject

Has Abstract

pub_date

1998-08-07 00:00:00

pages

179-81

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)00859-X

journal_volume

432

pub_type

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