Linked Life Data

9560424

Source:http://linkedlifedata.com/resource/pubmed/id/9560424

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1998-6-22
pubmed:databankReference
pubmed:abstractText
During growth with fumarate as the terminal electron transport acceptor and either formate or sulfide as the electron donor, Wolinella succinogenes induced a peri-plasmic protein (54 kDa) that reacted with an antiserum raised against the periplasmic fumarate reductase (Fcc) of Shewanella putrefaciens. However, the periplasmic cell fraction of W. succinogenes did not catalyze fumarate reduction with viologen radicals. W. succinogenes grown with polysulfide instead of fumarate contained much less (< 10%) of the 54-kDa antigen, and the antigen was not detectable in nitrate-grown bacteria. The antigen was most likely encoded by the fccA gene of W. succinogenes. The antigen was absent from a DeltafccABC mutant, and its size is close to that of the protein predicted by fccA. The fccA gene probably encodes a pre-protein carrying an N-terminal signal peptide. The sequence of the mature FccA (481 residues, 52.4 kDa) is similar (31% identity) to that of the C-terminal part (450 residues) of S. putrefaciens fumarate reductase. As indicated by Northern blot analysis, fccA is cotranscribed with fccB and fccC. The proteins predicted from the fccB and fccC gene sequences represent tetraheme cytochromes c. FccB is similar to the N-terminal part (150 residues) of S. putrefaciens fumarate reductase, while FccC resembles the tetraheme cytochromes c of the NirT/NapC family. The DeltafccABC mutant of W. succinogenes grew with fumarate and formate or sulfide, suggesting that the deleted proteins were not required for fumarate respiration with either electron donor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0302-8933
pubmed:author
pubmed:issnType
Print
pubmed:volume
169
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
424-33
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9560424-Amino Acid Sequence, pubmed-meshheading:9560424-Cell Membrane, pubmed-meshheading:9560424-Cytochrome c Group, pubmed-meshheading:9560424-Formic Acids, pubmed-meshheading:9560424-Fumarates, pubmed-meshheading:9560424-Genes, Bacterial, pubmed-meshheading:9560424-Gram-Negative Facultatively Anaerobic Rods, pubmed-meshheading:9560424-Molecular Sequence Data, pubmed-meshheading:9560424-Molecular Weight, pubmed-meshheading:9560424-Periplasm, pubmed-meshheading:9560424-RNA, Bacterial, pubmed-meshheading:9560424-RNA, Messenger, pubmed-meshheading:9560424-Restriction Mapping, pubmed-meshheading:9560424-Sequence Deletion, pubmed-meshheading:9560424-Sequence Homology, Amino Acid, pubmed-meshheading:9560424-Succinate Dehydrogenase, pubmed-meshheading:9560424-Sulfides, pubmed-meshheading:9560424-Wolinella
pubmed:year
1998
pubmed:articleTitle
A periplasmic flavoprotein in Wolinella succinogenes that resembles the fumarate reductase of Shewanella putrefaciens.
pubmed:affiliation
Institut für Mikrobiologie, Johann Wolfgang Goethe-Universität, Marie-Curie-Strasse 9, D-60439 Frankfurt am Main, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't