Site-directed mutational analysis of DnaA protein, the initiator of chromosomal DNA replication in E. coli

Tohru Mizushima

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

DnaA protein, the initiator for chromosomal DNA replication in Escherichia coli, has various activities, such as oligomerization (DnaA-DnaA interaction), ATP-binding, ATPase activity and membrane-binding. Site- directed mutational analyses have revealed not only the amino acid residues that are essential for these activities but also the functions of these activities. Following is a summary of the functions and regulatory mechanisms of DnaA protein in the initiation of chromosomal DNA replication. ATP-bound DnaA protein, but not other forms of the protein binds to the origin of DNA replication and forms oligomers to open-up the duplex DNA. This oligomerization is mediated by a DnaA-DnaA interaction through the N-terminal region of the protein. After initiation of DNA replication, the ATPase activity of DnaA protein is stimulated and DnaA protein is inactivated to the ADP-bound form to suppress the re-initiation of DNA replication. DnaA protein binds to acidic phospholipids through an ionic interaction between basic amino acid residues of the protein and acidic residues of phospholipids. This interaction seems to be involved in the re-activation of DnaA protein (from the ADP-bound form to the ATP-bound form) to initiate DNA replication after the appropriate interval.

Original languageEnglish
Pages (from-to)1-7
Number of pages7
JournalJournal of Biochemistry
Volume127
Issue number1
Publication statusPublished - 2000
Externally publishedYes

Fingerprint

DNA Replication
Escherichia coli
DNA
Proteins
Oligomerization
Adenosine Triphosphate
Adenosine Diphosphate
Adenosine Triphosphatases
Phospholipids
Basic Amino Acids
Replication Origin
Essential Amino Acids
Oligomers
Chemical activation
Membranes
Amino Acids

Keywords

  • Chromosomal DNA replication
  • DnaA protein
  • Escherichia coli
  • ORC
  • Site- directed mutation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Site-directed mutational analysis of DnaA protein, the initiator of chromosomal DNA replication in E. coli. / Mizushima, Tohru.

In: Journal of Biochemistry, Vol. 127, No. 1, 2000, p. 1-7.

Research output: Contribution to journalArticle

@article{37175bf1ff1c49e1a951d1a70ff6bdfa,
title = "Site-directed mutational analysis of DnaA protein, the initiator of chromosomal DNA replication in E. coli",
abstract = "DnaA protein, the initiator for chromosomal DNA replication in Escherichia coli, has various activities, such as oligomerization (DnaA-DnaA interaction), ATP-binding, ATPase activity and membrane-binding. Site- directed mutational analyses have revealed not only the amino acid residues that are essential for these activities but also the functions of these activities. Following is a summary of the functions and regulatory mechanisms of DnaA protein in the initiation of chromosomal DNA replication. ATP-bound DnaA protein, but not other forms of the protein binds to the origin of DNA replication and forms oligomers to open-up the duplex DNA. This oligomerization is mediated by a DnaA-DnaA interaction through the N-terminal region of the protein. After initiation of DNA replication, the ATPase activity of DnaA protein is stimulated and DnaA protein is inactivated to the ADP-bound form to suppress the re-initiation of DNA replication. DnaA protein binds to acidic phospholipids through an ionic interaction between basic amino acid residues of the protein and acidic residues of phospholipids. This interaction seems to be involved in the re-activation of DnaA protein (from the ADP-bound form to the ATP-bound form) to initiate DNA replication after the appropriate interval.",
keywords = "Chromosomal DNA replication, DnaA protein, Escherichia coli, ORC, Site- directed mutation",
author = "Tohru Mizushima",
year = "2000",
language = "English",
volume = "127",
pages = "1--7",
journal = "Journal of Biochemistry",
issn = "0021-924X",
publisher = "Oxford University Press",
number = "1",

}

TY - JOUR

T1 - Site-directed mutational analysis of DnaA protein, the initiator of chromosomal DNA replication in E. coli

AU - Mizushima, Tohru

PY - 2000

Y1 - 2000

N2 - DnaA protein, the initiator for chromosomal DNA replication in Escherichia coli, has various activities, such as oligomerization (DnaA-DnaA interaction), ATP-binding, ATPase activity and membrane-binding. Site- directed mutational analyses have revealed not only the amino acid residues that are essential for these activities but also the functions of these activities. Following is a summary of the functions and regulatory mechanisms of DnaA protein in the initiation of chromosomal DNA replication. ATP-bound DnaA protein, but not other forms of the protein binds to the origin of DNA replication and forms oligomers to open-up the duplex DNA. This oligomerization is mediated by a DnaA-DnaA interaction through the N-terminal region of the protein. After initiation of DNA replication, the ATPase activity of DnaA protein is stimulated and DnaA protein is inactivated to the ADP-bound form to suppress the re-initiation of DNA replication. DnaA protein binds to acidic phospholipids through an ionic interaction between basic amino acid residues of the protein and acidic residues of phospholipids. This interaction seems to be involved in the re-activation of DnaA protein (from the ADP-bound form to the ATP-bound form) to initiate DNA replication after the appropriate interval.

AB - DnaA protein, the initiator for chromosomal DNA replication in Escherichia coli, has various activities, such as oligomerization (DnaA-DnaA interaction), ATP-binding, ATPase activity and membrane-binding. Site- directed mutational analyses have revealed not only the amino acid residues that are essential for these activities but also the functions of these activities. Following is a summary of the functions and regulatory mechanisms of DnaA protein in the initiation of chromosomal DNA replication. ATP-bound DnaA protein, but not other forms of the protein binds to the origin of DNA replication and forms oligomers to open-up the duplex DNA. This oligomerization is mediated by a DnaA-DnaA interaction through the N-terminal region of the protein. After initiation of DNA replication, the ATPase activity of DnaA protein is stimulated and DnaA protein is inactivated to the ADP-bound form to suppress the re-initiation of DNA replication. DnaA protein binds to acidic phospholipids through an ionic interaction between basic amino acid residues of the protein and acidic residues of phospholipids. This interaction seems to be involved in the re-activation of DnaA protein (from the ADP-bound form to the ATP-bound form) to initiate DNA replication after the appropriate interval.

KW - Chromosomal DNA replication

KW - DnaA protein

KW - Escherichia coli

KW - ORC

KW - Site- directed mutation

UR - http://www.scopus.com/inward/record.url?scp=0033983659&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033983659&partnerID=8YFLogxK

M3 - Article

C2 - 10731659

AN - SCOPUS:0033983659

VL - 127

SP - 1

EP - 7

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 1

ER -