Site-directed mutational analysis for the membrane binding of DnaA protein. Identification of amino acids involved in the functional interaction between DnaA protein and acidic phospholipids.
about
Mutations in DnaA protein suppress the growth arrest of acidic phospholipid-deficient Escherichia coli cells.The antifungal protein AFP of Aspergillus giganteus is an oligonucleotide/oligosaccharide binding (OB) fold-containing protein that produces condensation of DNA.Analysis on origin recognition complex containing Orc5p with defective Walker A motif.Amphitropic proteins: regulation by reversible membrane interactions (review).Association of the chromosome replication initiator DnaA with the Escherichia coli inner membrane in vivo: quantity and mode of binding.Crosstalk between DnaA protein, the initiator of Escherichia coli chromosomal replication, and acidic phospholipids present in bacterial membranes.Common domains in the initiators of DNA replication in Bacteria, Archaea and Eukarya: combined structural, functional and phylogenetic perspectives.Domain structure and lipid interaction of recombinant yeast Tim44Separate roles of Escherichia coli replication proteins in synthesis and partitioning of pSC101 plasmid DNAInhibitory effects of acidic phospholipids on the binding of origin-recognition complex to origin DNA.Involvement of Arg-328, Arg-334 and Arg-342 of DnaA protein in the functional interaction with acidic phospholipids.Conserved hydrophobic amino acid residues in the N-terminal region of DnaA protein are involved in DnaA-DnaA interaction.Biochemical analysis of DnaA protein with mutations in both Arg328 and Lys372.Molecular mechanism for functional interaction between DnaA protein and acidic phospholipids: identification of important amino acids.Acidic phospholipids inhibit the DNA-binding activity of DnaA protein, the initiator of chromosomal DNA replication in Escherichia coli.Kinetics of ATP binding to the origin recognition complex of Saccharomyces cerevisiae.Restoration of growth to acidic phospholipid-deficient cells by DnaA(L366K) is independent of its capacity for nucleotide binding and exchange and requires DnaA.Membrane-catalyzed nucleotide exchange on DnaA. Effect of surface molecular crowding.Replicate Once Per Cell Cycle: Replication Control of Secondary Chromosomes
P2860
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P2860
Site-directed mutational analysis for the membrane binding of DnaA protein. Identification of amino acids involved in the functional interaction between DnaA protein and acidic phospholipids.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Site-directed mutational analy ...... tein and acidic phospholipids.
@en
type
label
Site-directed mutational analy ...... tein and acidic phospholipids.
@en
prefLabel
Site-directed mutational analy ...... tein and acidic phospholipids.
@en
P2093
P2860
P356
P1476
Site-directed mutational analy ...... tein and acidic phospholipids.
@en
P2093
Ishikawa Y
Mizushima T
Tsuchiya T
Yamaguchi Y
P2860
P304
28651-28656
P356
10.1074/JBC.273.44.28651
P407
P577
1998-10-01T00:00:00Z