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Nucleotide sequence encoding the flavoprotein and the iron-sulfur protein subunits of the Bacillus subtilis PY79 succinate dehydrogenase complex

Phillips, Mary K.; Hederstedt, Lars LU ; Hasnain, Shahida; Rutberg, Lars and Guest, J. (1987) In Journal of Bacteriology 169(2). p.864-873
Abstract
The nucleotide sequence of a 2.7-kilobase segment of DNA containing the sdhA and sdhB genes encoding the flavoprotein (Fp, sdhA) and iron-sulfur protein (Ip, sdhB) subunits of the succinate dehydrogenase of Bacillus subtilis was determined. This sequence extends the previously reported sequence encoding the cytochrome b558 subunit (sdhC) and completes the sequence of the sdh operon, sdhCAB. The predicted molecular weights for the Fp and Ip subunits, 65,186 (585 amino acids) and 28,285 (252 amino acids), agreed with the values determined independently for the labeled Fp and Ip antigens, although it appeared that the B. subtilis Fp was not functional after expression of the sdhA gene in Escherichia coli. Both subunits closely resembled the... (More)
The nucleotide sequence of a 2.7-kilobase segment of DNA containing the sdhA and sdhB genes encoding the flavoprotein (Fp, sdhA) and iron-sulfur protein (Ip, sdhB) subunits of the succinate dehydrogenase of Bacillus subtilis was determined. This sequence extends the previously reported sequence encoding the cytochrome b558 subunit (sdhC) and completes the sequence of the sdh operon, sdhCAB. The predicted molecular weights for the Fp and Ip subunits, 65,186 (585 amino acids) and 28,285 (252 amino acids), agreed with the values determined independently for the labeled Fp and Ip antigens, although it appeared that the B. subtilis Fp was not functional after expression of the sdhA gene in Escherichia coli. Both subunits closely resembled the corresponding Fp and Ip subunits of the succinate dehydrogenase (SDH) and fumarate reductase of E. coli in size, composition, and amino acid sequence. The sequence homologies further indicated that the B. subtilis SDH subunits are equally related to the SDH and fumarate reductase subunits of E. coli but are less closely related than are the corresponding pairs of E. coli subunits. The regions of highest sequence conservation were identifiable as the catalytically significant flavin adenine dinucleotide-binding sites and cysteine clusters of the iron-sulfur centers. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Bacteriology
volume
169
issue
2
pages
864 - 873
publisher
American Society for Microbiology
ISSN
0021-9193
DOI
10.1128/jb.169.2.864-873.1987
language
English
LU publication?
no
id
c73edb0b-0780-40f1-a3fc-6f5e746f6f15
date added to LUP
2017-07-18 11:02:38
date last changed
2017-11-14 09:51:04
@article{c73edb0b-0780-40f1-a3fc-6f5e746f6f15,
  abstract     = {The nucleotide sequence of a 2.7-kilobase segment of DNA containing the sdhA and sdhB genes encoding the flavoprotein (Fp, sdhA) and iron-sulfur protein (Ip, sdhB) subunits of the succinate dehydrogenase of Bacillus subtilis was determined. This sequence extends the previously reported sequence encoding the cytochrome b558 subunit (sdhC) and completes the sequence of the sdh operon, sdhCAB. The predicted molecular weights for the Fp and Ip subunits, 65,186 (585 amino acids) and 28,285 (252 amino acids), agreed with the values determined independently for the labeled Fp and Ip antigens, although it appeared that the B. subtilis Fp was not functional after expression of the sdhA gene in Escherichia coli. Both subunits closely resembled the corresponding Fp and Ip subunits of the succinate dehydrogenase (SDH) and fumarate reductase of E. coli in size, composition, and amino acid sequence. The sequence homologies further indicated that the B. subtilis SDH subunits are equally related to the SDH and fumarate reductase subunits of E. coli but are less closely related than are the corresponding pairs of E. coli subunits. The regions of highest sequence conservation were identifiable as the catalytically significant flavin adenine dinucleotide-binding sites and cysteine clusters of the iron-sulfur centers. },
  author       = {Phillips, Mary K. and Hederstedt, Lars and Hasnain, Shahida and Rutberg, Lars and Guest, J.},
  issn         = {0021-9193},
  language     = {eng},
  number       = {2},
  pages        = {864--873},
  publisher    = {American Society for Microbiology},
  series       = {Journal of Bacteriology},
  title        = {Nucleotide sequence encoding the flavoprotein and the iron-sulfur protein subunits of the<em> Bacillus subtilis</em> PY79 succinate dehydrogenase complex},
  url          = {http://dx.doi.org/10.1128/jb.169.2.864-873.1987},
  volume       = {169},
  year         = {1987},
}