Document Detail


Mutations in DnaA protein suppress the growth arrest of acidic phospholipid-deficient Escherichia coli cells.
MedLine Citation:
PMID:  11230139     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cell growth arrests when the concentrations of anionic phospholipids drop below a critical level in Escherichia coli, with the insufficient amounts of acidic phospholipids adversely affecting the DnaA-dependent initiation of DNA replication at the chromosomal origin (oriC). Mutations have been introduced into the carboxyl region of DnaA, including the portion identified as essential for productive in vitro DnaA-acidic phospholipid interactions. Expression of DnaA proteins possessing certain small deletions or substituted amino acids restored growth to cells deficient in acidic phospholipids, whereas expression of wild-type DnaA did not. The mutations include substitutions and deletions in the phospholipid-interacting domain as well as some small deletions in the DNA-binding domain of DnaA. Marker frequency analysis indicated that initiation of replication occurs at or near oriC in acidic phospholipid- deficient cells rescued by the expression of DnaA having a point mutation in the membrane-binding domain, DnaA(L366K). Flow cytometry revealed that expression in wild-type cells of plasmid-borne DnaA(L366K) and DnaA(Delta363-367) reduced the frequency with which replication was initiated and disturbed the synchrony of initiations.
Authors:
W Zheng; Z Li; K Skarstad; E Crooke
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The EMBO journal     Volume:  20     ISSN:  0261-4189     ISO Abbreviation:  EMBO J.     Publication Date:  2001 Mar 
Date Detail:
Created Date:  2001-03-20     Completed Date:  2001-04-19     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  8208664     Medline TA:  EMBO J     Country:  England    
Other Details:
Languages:  eng     Pagination:  1164-72     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, Georgetown University Medical Center, 3900 Reservoir Road NW, Washington DC 20007, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Substitution / genetics
Bacterial Proteins / analysis,  chemistry,  genetics*,  metabolism*
Cell Division
Cephalexin / pharmacology
Chromosomes, Bacterial / genetics
DNA Replication / drug effects
DNA, Bacterial / biosynthesis,  genetics
DNA-Binding Proteins / chemistry,  genetics*,  metabolism*
Escherichia coli / cytology*,  genetics,  growth & development,  metabolism
Flow Cytometry
Hydrogen-Ion Concentration
Origin Recognition Complex
Phospholipids / chemistry,  deficiency*
Plasmids / genetics
Protein Structure, Tertiary
Rifampin / pharmacology
Sequence Deletion / genetics
Suppression, Genetic / genetics*
Transformation, Bacterial
Viral Proteins / genetics
Grant Support
ID/Acronym/Agency:
GM49700/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/DNA, Bacterial; 0/DNA-Binding Proteins; 0/DnaA protein, Bacteria; 0/OriC chromosomal replication origin; 0/Origin Recognition Complex; 0/Phospholipids; 0/Viral Proteins; 13292-46-1/Rifampin; 15686-71-2/Cephalexin
Comments/Corrections

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