1987
DOI: 10.1128/jb.169.2.864-873.1987
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Nucleotide sequence encoding the flavoprotein and iron-sulfur protein subunits of the Bacillus subtilis PY79 succinate dehydrogenase complex

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 BaciUus 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 The structural genes encoding the subunits of the SDH complex form an operon at 225°on the B. subtilis linkage map (… Show more

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Cited by 107 publications
(59 citation statements)
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“…The three polypeptides of the B. subtilis SDH-cytochrome b-558 complex are expressed from plasmid pSH1047 in E. coli, but the functional complex is not assembled [9]. Fp and Ip are found in the cytoplasm, whereas cytochrome b-558 with normal physico-chemical properties is found in the inner membrane.…”
Section: B Subtilis Fp Expressed In E Coli Is Defectivementioning
confidence: 99%
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“…The three polypeptides of the B. subtilis SDH-cytochrome b-558 complex are expressed from plasmid pSH1047 in E. coli, but the functional complex is not assembled [9]. Fp and Ip are found in the cytoplasm, whereas cytochrome b-558 with normal physico-chemical properties is found in the inner membrane.…”
Section: B Subtilis Fp Expressed In E Coli Is Defectivementioning
confidence: 99%
“…The cytochrome spans the lipid bilayer and anchors Correspondence address: L. Hederstedt, Dept of Microbiology, University of Lund, SGlvegatan 21, S-223 62 Lund, Sweden SDH to the inner surface of the cytoplasmic membrane [7]. The nucleotide sequence of the genes coding for Fp, Ip, and cytochrome b-558 was recently determined from the cloned B. subtilis sdhCAB operon [8,9]. To confirm each of the reading frames predicted from the DNA sequence and to determine possible N-terminal posttranslational processings of the subunits, we have studied the proteins by radiosequence analysis.…”
Section: Introductionmentioning
confidence: 99%
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“…2B). Another segment interacting with the AMP moiety is the stretch from residues 357 to 386 in E. coli sdhA [8] and from residues 355 to 374 in B. subtilis sdhA [11]. To see if this segment is also detectable in the Ascaris Fp subunit, 20 out of the 40 tryptic peptides of the Fp subunit were partially sequenced, since the Lys residues in the amino terminal part of the segment in bacterial Fp (Lys-343 in E. coli sdhA and Lys-341 in B. subtilis sdhA) are well-conserved and trypsin specifically digests the C-terminal of Lys and Arg residues in the a From the results reported in [20] b From the results reported in [8] c From the results reported in [10] a Calculated according to [21] peptide.…”
Section: Resultsmentioning
confidence: 99%
“…It is a major component of Ascaris mitochondria (8o70 of mitochondrial protein) [7] and is composed of the following four subunits: a flavoprotein (Fp) subunit containing a flavin (Mr= 68 kDa), an Ip subunit associated with iron-sulfur centers (Mr = 26 kDa) and two hydrophobic, heme bcontaining polypeptides called CybL and Cybs (Mr = 15 and 13.5 kDa, respectively) [3,5]. In the case of bacteria, the genes of complex II have been cloned and sequenced from Escherichia coil (sdh and frd) [8][9][10], Bacillus subtilis (sdh ) [11,12] and Proteus vulgaris (frd) [13]. Structural information on mitochondrial complex…”
Section: Introductionmentioning
confidence: 99%