11102450

Source:http://linkedlifedata.com/resource/pubmed/id/11102450

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0001128, umls-concept:C0002520, umls-concept:C0020792, umls-concept:C0031676, umls-concept:C0033684, umls-concept:C0205245, umls-concept:C0441712, umls-concept:C1521991, umls-concept:C1704675
pubmed:issue	10
pubmed:dateCreated	2001-5-25
pubmed:abstractText	DnaA protein, the initiator of chromosomal DNA replication in Escherichia coli, seems to be reactivated from the ADP-bound form to its ATP-bound form through stimulation of ADP release by acidic phospholipids such as cardiolipin. We previously reported that two potential amphipathic helices (Lys-327 to Ile-344 and Asp-357 to Val-374) of DnaA protein are involved in the functional interaction between DnaA and cardiolipin. In relation to one of these helices (Asp-357 to Val-374), we demonstrated that basic amino acids in the helix, especially Lys-372, are vital for this interaction. In this study, we have identified an amino acid in the second potential amphipathic helix (Lys-327 to Ile-344), which would also appear to be involved in the interaction. We constructed three mutant dnaA genes with a single mutation (dnaAR328E, dnaAR334E, and dnaAR342E) and examined the function of the mutant proteins. DnaAR328E, but not DnaAR334E and DnaAR342E, was found to be more resistant to inhibition of its ATP binding activity by cardiolipin than the wild-type protein. The stimulation of ADP release from DnaAR328E by cardiolipin was also weaker than that observed with the other mutants and the wild-type protein. These results suggest that Arg-328 of DnaA protein is involved in the functional interaction of this protein with acidic phospholipids. We propose that acidic phospholipids bind to two basic amino acid residues (Arg-328 and Lys-372) of DnaA protein and change the higher order structure of its ATP-binding pocket, which in turn stimulates the release of ADP from the protein.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/2985121R
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Adenine, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cardiolipins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DnaA protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/Isoleucine, http://linkedlifedata.com/resource/pubmed/chemical/Lysine, http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids, http://linkedlifedata.com/resource/pubmed/chemical/Valine
pubmed:status	MEDLINE
pubmed:month	Mar
pubmed:issn	0021-9258
pubmed:author	pubmed-author:LynnA MAM, pubmed-author:MakiseMM, pubmed-author:MizushimaTT, pubmed-author:TsuchiyaTT
pubmed:issnType	Print
pubmed:day	9
pubmed:volume	276
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	7450-6
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:11102450-Adenine, pubmed-meshheading:11102450-Adenosine Diphosphate, pubmed-meshheading:11102450-Adenosine Triphosphate, pubmed-meshheading:11102450-Amino Acid Sequence, pubmed-meshheading:11102450-Aspartic Acid, pubmed-meshheading:11102450-Bacterial Proteins, pubmed-meshheading:11102450-Base Sequence, pubmed-meshheading:11102450-Cardiolipins, pubmed-meshheading:11102450-DNA-Binding Proteins, pubmed-meshheading:11102450-Dose-Response Relationship, Drug, pubmed-meshheading:11102450-Escherichia coli, pubmed-meshheading:11102450-Isoleucine, pubmed-meshheading:11102450-Lysine, pubmed-meshheading:11102450-Models, Biological, pubmed-meshheading:11102450-Molecular Sequence Data, pubmed-meshheading:11102450-Mutagenesis, Site-Directed, pubmed-meshheading:11102450-Mutation, pubmed-meshheading:11102450-Phospholipids, pubmed-meshheading:11102450-Plasmids, pubmed-meshheading:11102450-Protein Binding, pubmed-meshheading:11102450-Time Factors, pubmed-meshheading:11102450-Valine
pubmed:year	2001
pubmed:articleTitle	Molecular mechanism for functional interaction between DnaA protein and acidic phospholipids: identification of important amino acids.
pubmed:affiliation	Faculty of Pharmaceutical Sciences, Okayama University, and PRESTO, Japan Science and Technology Corporation, Okayama 700-8530, Japan.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't