Processing of Bacillus subtilis succinate dehydrogenase and cytochrome &‐558 polypeptides

FEBS Letters

Hederstedt, Lars¹  Bergman, Tomas¹  Jörnvall, Hans¹ 

[1] Department of Microbiology, University of Lund, Sölvegatan 21, S-223 62 Lund and Department of Chemistry I, Karolinska Institutet, S-104 01 Stockholm, Sweden

关键词: Succinate dehydrogenase;    Post-translational processing;    Heterologous system;    Electroblotting;    Radiosequence analysis;    N-terminal heterogeneity;   

DOI  :  10.1016/0014-5793(87)81527-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown