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Processing of Bacillus subtilis succinate dehydrogenase and cytochrome b-558 polypeptides

Hederstedt, Lars LU ; Bergman, Tomas and Jörnvall, H. (1987) In FEBS Letters 213. p.385-390
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... (More)
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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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
FEBS Letters
volume
213
pages
385 - 390
publisher
Wiley-Blackwell
external identifiers
  • scopus:0023099325
ISSN
1873-3468
DOI
10.1016/0014-5793(87)81527-2
language
English
LU publication?
yes
id
402e6247-dc97-4133-ac8a-24012e104d9c
date added to LUP
2017-07-18 11:00:23
date last changed
2017-10-08 05:05:05
@article{402e6247-dc97-4133-ac8a-24012e104d9c,
  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.<br/>},
  author       = {Hederstedt, Lars and Bergman, Tomas and Jörnvall, H.},
  issn         = {1873-3468},
  language     = {eng},
  pages        = {385--390},
  publisher    = {Wiley-Blackwell},
  series       = {FEBS Letters},
  title        = {Processing of <em>Bacillus subtilis</em> succinate dehydrogenase and cytochrome b-558 polypeptides},
  url          = {http://dx.doi.org/10.1016/0014-5793(87)81527-2},
  volume       = {213},
  year         = {1987},
}