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A dnaB-like protein of Pseudomonas aeruginosa.

Abstract：

:A dnaB-like protein from P. aeruginosa was purified to near homogeneity using as an assay the immunoprecipitation by E. coli dnaB antiserum in a solid-phase. In the chromatographic characteristics including the affinity to immobilized ATP the dnaB-like protein of P. aeruginosa is similar to the dnaB protein of E. coli with the exception that it does not bind to heparin-Sepharose. The dnaB-like protein has a native molecular weight of about 320,000 as determined by glycerol gradient sedimentation. It consists of several identical subunits of molecular weight of 56,000 as measured in a denaturing SDS gel. Associated with the enzyme is a DNA-dependent ATPase- and helicase activity. The dnaB-like protein is similar to the E. coli dnaB protein with regard to the binding of ATP gamma S and the formation of a ternary complex consisting of the enzyme, ATP gamma S, and phi X174 DNA. However, the enzyme of P. aeruginosa is inactive in a phi X174 DNA-dependent in vitro dnaB complementation assay using an E. coli dnaBts extract.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Dreiseikelmann B,Riedel HD,Schuster H

doi

10.1093/nar/15.2.385

subject

Has Abstract

pub_date

1987-01-26 00:00:00

pages

385-95

issue

2

eissn

0305-1048

issn

1362-4962

journal_volume

15

pub_type

杂志文章

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