Processing of Bacillus subtilis succinate dehydrogenase and cytochrome b-558 polypeptides
(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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Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/402e6247-dc97-4133-ac8a-24012e104d9c
- author
- Hederstedt, Lars LU ; Bergman, Tomas and Jörnvall, H.
- organization
- publishing date
- 1987
- 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
- 2021-02-07 06:11:39
@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}}, doi = {{10.1016/0014-5793(87)81527-2}}, volume = {{213}}, year = {{1987}}, }