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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
38
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pubmed:dateCreated |
1995-10-17
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pubmed:databankReference | |
pubmed:abstractText |
The Dps family of proteins are a diverse group of bacterial stress-inducible polypeptides that bind DNA and likely confer resistance to peroxide damage during periods of oxidative stress and long term nutrient limitation. Some members of the Dps protein family have been shown to form large (approximately 150-kDa), hexameric complexes that bind chromosomal DNA with little sequence specificity. In this paper we report the nucleotide sequence of the dpsA gene from Synechococcus sp. PCC7942 encoding a cyanobacterial Dps homolog. The deduced amino acid sequence of the Synechococcus sp. DpsA protein revealed that a carboxyl-terminal domain of the protein was > 60% homologous to the COOH-terminal half of bacterioferritin. Other known Dps family members lack such high similarity to the bacterioferritins. Purification and spectroscopic analysis of the Synechococcus sp. DpsA protein complex revealed that the complex contains heme and has a weak catalase activity in vitro. Activity staining of nondenaturing polyacrylamide gels showed that the protein complex comigrated with both the heme and the catalase activity, and O2 evolution measurements yielded a maximal specific activity of 1.7 mumol of H2O2 consumed/micrograms of protein-1 min-1. We speculate that the protein may have a peroxide-consuming mechanism located on the chromosomal DNA, and we also suggest that this activity may be a necessary feature to handle the endogenous oxidative stresses associated with oxygenic photosynthesis. Last, the evolutionary link between the Dps protein family and the bacterioferritins is discussed.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Catalase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DPS protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hemeproteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
22478-82
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7673237-Amino Acid Sequence,
pubmed-meshheading:7673237-Bacterial Proteins,
pubmed-meshheading:7673237-Base Sequence,
pubmed-meshheading:7673237-Catalase,
pubmed-meshheading:7673237-Consensus Sequence,
pubmed-meshheading:7673237-Cyanobacteria,
pubmed-meshheading:7673237-DNA-Binding Proteins,
pubmed-meshheading:7673237-Heat-Shock Proteins,
pubmed-meshheading:7673237-Hemeproteins,
pubmed-meshheading:7673237-Molecular Sequence Data,
pubmed-meshheading:7673237-Molecular Weight,
pubmed-meshheading:7673237-Sequence Alignment,
pubmed-meshheading:7673237-Sequence Homology, Amino Acid,
pubmed-meshheading:7673237-Spectrum Analysis
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pubmed:year |
1995
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pubmed:articleTitle |
The DpsA protein of Synechococcus sp. Strain PCC7942 is a DNA-binding hemoprotein. Linkage of the Dps and bacterioferritin protein families.
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pubmed:affiliation |
Department of Biological Sciences, Bowling Green State University, Ohio 43403-0212, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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