Processing of Bacillus subtilis succinate dehydrogenase and cytochrome b-558 polypeptides. Lack of covalently bound flavin in the Bacillus enzyme expressed in Escherichia coli.
FEBS Lett
; 213(2): 385-90, 1987 Mar 23.
Article
em En
| MEDLINE
| ID: mdl-3104091
ABSTRACT
The DNA sequence of the Bacillus subtilis sdh operon coding for the two succinate dehydrogenase subunits and cytochrome b-558 (the membrane anchor protein) has recently been established. We have now determined the extent of N-terminal processing of each polypeptide by radiosequence analysis. At the same time, direct evidence for the correctness of the predicted reading frames has been obtained. The cytochrome showed a ragged N-terminus, with forms lacking one residue, and is inserted across the membrane without an N-terminal leader-peptide. Covalently bound flavin was not detectable in B. subtilis succinate dehydrogenase expressed in Escherichia coli despite normal N-terminal processing of the apoprotein. This provides an explanation to why the succinate dehydrogenase synthesized in E. coli is not functional and demonstrates that host-specific factors regulate the coenzyme attachment.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Succinato Desidrogenase
/
Bacillus subtilis
/
Processamento de Proteína Pós-Traducional
/
NADPH Oxidases
/
Grupo dos Citocromos b
/
Escherichia coli
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1987
Tipo de documento:
Article