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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1998-12-11
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pubmed:databankReference | |
pubmed:abstractText |
Sponges (Porifera) are the phylogenetically oldest metazoan organisms. From one member of the siliceous sponges, Geodia cydonium, the cDNA encoding a putative SOS protein, the AidB-like protein of the Ada system from bacteria, was isolated and characterized. The cDNA, GCaidB, comprises an open reading frame of 446 amino acid (aa) residues encoding a polypeptide with a calculated Mr of 49,335. This molecule shows high similarity to the bacterial AidB proteins from Mycobacterium tuberculosis and Escherichia coli and somewhat lower similarities to acyl-CoA dehydrogenases (ADHs) and acyl-CoA oxidases (AOXs). Northern blot analysis confirmed the presence of the complete transcript. The deduced sponge aa sequence, GC_aidB, possesses the two characteristic acyl-CoA dehydrogenase signatures 1 and 2. Incubation of the sponge with N-methyl-N'-nitro-N-nitrosoguanidine causes a strong increase in the 2.1-kb large transcript of GCaidB; maximal expression is seen after 24 h of incubation with this DNA methylating agent. ADHs and AOXs can be grouped, depending on the position of the catalytically important Glu residue, into the Glu-Gly (Glu adjacent to Gly) class and the Glu-Arg (Glu adjacent to Arg) class. The phylogenetically oldest metazoan AidB-like molecule, GC_aidB of G. cydonium, belongs to the Glu-Gly class of ADHs. Phylogenetic analyses of the Glu-Gly class enzymes, with the described AidB-like protein from G. cydonium and the bacterial AidB polypeptides, together with metazoan ADHs and AOXs, revealed that the AidB(-like) proteins diverged first from a common ancestor, while the eukaryotic AOX and ADA polypeptides as well as the GHDs appeared later. According to the analyses, the very long-chain ADHs are older than the medium-chain, short-chain, and branched-chain ADHs. Inclusion of the phylogenetical oldest member of the Glu-Arg class of enzymes, the bacterial ADH-CaiA sequence in these analyses, revealed that this class of enzymes appeared later in evolution and arose from the Glu-Gly class perhaps after gene duplication.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acyl-CoA Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Acyl-CoA Dehydrogenase, Long-Chain,
http://linkedlifedata.com/resource/pubmed/chemical/AidB protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0022-2844
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
47
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
343-52
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9732461-Acyl-CoA Dehydrogenase,
pubmed-meshheading:9732461-Acyl-CoA Dehydrogenase, Long-Chain,
pubmed-meshheading:9732461-Amino Acid Sequence,
pubmed-meshheading:9732461-Animals,
pubmed-meshheading:9732461-Bacterial Proteins,
pubmed-meshheading:9732461-Base Sequence,
pubmed-meshheading:9732461-Blotting, Northern,
pubmed-meshheading:9732461-DNA, Complementary,
pubmed-meshheading:9732461-Escherichia coli Proteins,
pubmed-meshheading:9732461-Evolution, Molecular,
pubmed-meshheading:9732461-Invertebrates,
pubmed-meshheading:9732461-Molecular Sequence Data,
pubmed-meshheading:9732461-Oxidoreductases,
pubmed-meshheading:9732461-Phylogeny,
pubmed-meshheading:9732461-Porifera,
pubmed-meshheading:9732461-SOS Response (Genetics),
pubmed-meshheading:9732461-Sequence Alignment,
pubmed-meshheading:9732461-Sequence Analysis, DNA
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pubmed:year |
1998
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pubmed:articleTitle |
Identification and expression of the SOS response, aidB-like, gene in the marine sponge Geodia cydonium: implication for the phylogenetic relationships of metazoan acyl-CoA dehydrogenases and acyl-CoA oxidases.
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pubmed:affiliation |
Institut für Physiologische Chemie, Abteilung für Angewandte Molekularbiologie, Universität, Duesbergweg 6, D-55099 Mainz, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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