| Restoration of growth to acidic phospholipid-deficient cells by DnaA(L366K) is independent of its capacity for nucleotide binding and exchange and requires DnaA. | |
| | |
MedLine Citation:
|
PMID: 15642730 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
In the absence of adequate levels of cellular acidic phospholipids, Escherichia coli remain viable but are arrested for growth. Expression of a DnaA protein that contains a single amino acid substitution in the membrane-binding domain, DnaA(L366K), in concert with expression of wild-type DnaA protein, restores growth. DnaA protein has high affinity for ATP and ADP, and in vitro lipid bilayers that are fluid and contain acidic phospholipids reactivate inert ADP-DnaA by promoting an exchange of ATP for ADP. Here, nucleotide and lipid interactions and replication activity of purified DnaA(L366K) were examined to gain insight into the mechanism of how it restores growth to cells lacking acidic phospholipids. DnaA(L366K) behaved like wild-type DnaA with respect to nucleotide binding affinities and hydrolysis properties, specificity of acidic phospholipids for nucleotide release, and origin binding. Yet, DnaA(L366K) was feeble at initiating replication from oriC unless augmented with a limiting quantity of wild-type DnaA, reflecting the in vivo requirement that both wild-type and a mutant form of DnaA must be expressed and act together to restore growth to acidic phospholipid deficient cells. |
| | |
Authors:
|
Zhenya Li; Jennifer L Kitchen; Kelly Boeneman; Priyanka Anand; Elliott Crooke |
Publication Detail:
|
Type: Journal Article; Research Support, U.S. Gov't, P.H.S. Date: 2005-01-10 |
Journal Detail:
|
Title: The Journal of biological chemistry Volume: 280 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2005 Mar |
Date Detail:
|
Created Date: 2005-03-14 Completed Date: 2005-04-25 Revised Date: 2007-11-14 |
Medline Journal Info:
|
Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
|
Languages: eng Pagination: 9796-801 Citation Subset: IM |
Affiliation:
|
Department of Biochemistry and Molecular Biology, Georgetown University Medical Center, 3900 Reservoir Rd. NW, Washington, DC 20007, USA. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Adenosine Diphosphate
/
chemistry Adenosine Triphosphate / chemistry Bacterial Proteins / genetics, metabolism* Cell-Free System Chromosomes / metabolism Chromosomes, Bacterial DNA Replication DNA-Binding Proteins / genetics, metabolism* Dose-Response Relationship, Drug Escherichia coli / metabolism* Hydrolysis Lipid Bilayers / chemistry Lipid Metabolism Lipids / chemistry Mutation Phospholipids / chemistry, metabolism Protein Binding Protein Structure, Tertiary Replication Origin Time Factors |
| Grant Support | |
ID/Acronym/Agency:
|
R01GM49700/GM/NIGMS NIH HHS; T32CA009686/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
|
0/Bacterial Proteins; 0/DNA-Binding Proteins; 0/DnaA protein, Bacteria; 0/Lipid Bilayers; 0/Lipids; 0/Phospholipids; 56-65-5/Adenosine Triphosphate; 58-64-0/Adenosine Diphosphate |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Phosphoinositide 3-kinase is required for intracellular Listeria monocytogenes actin-based motility ...
Next Document: The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the pro...