TY  - JOUR
AB  - 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.
DA  - 1987
DO  - 10.1093/nar/15.2.385  1773912
LA  - eng
IS  - 2
M2  - 385
PY  - 1987
SN  - 0305-1048
SP  - 385-395
T2  - Nucleic Acids Research
TI  - A dnaB-like protein of Pseudomonas aeruginosa
UR  - https://nbn-resolving.org/urn:nbn:de:0070-bipr-16422
Y2  - 2024-11-22T05:00:36
ER  -