High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D.

Abstract:

:The formation of cytoplasmic inclusion bodies by Escherichia coli overproducing Clostridium thermocellum endoglucanase D (EGD) was investigated. EGD was found in inclusion bodies as a 68 kDa form, whereas the size of the cytoplasmic form was 65 kDa. Upon solubilization with urea followed by dialysis, the 68 kDa form was converted to the 65 kDa species. Proteolysis occurred within the COOH-terminal, reiterated region of the 68 kDa form, which is conserved among most C. thermocellum endoglucanases, but is not required for catalytic activity. The specific activity of the enzyme embedded in inclusion bodies was close to that of the purified protein. Thus, inclusion body formation does not involve denaturation of the catalytic domain of EGD, but, more likely, the participation of the reiterated, conserved region in intermolecular interactions.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Tokatlidis K,Dhurjati P,Millet J,Béguin P,Aubert JP

doi

10.1016/0014-5793(91)80478-l

subject

Has Abstract

pub_date

1991-04-22 00:00:00

pages

205-8

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)80478-L

journal_volume

282

pub_type

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