Isolation and properties of the RepA1 protein of the IncFII replicon, RepFIC.
The initiator protein RepA1 of the IncFII replicon RepFIC derived from the enterotoxin plasmid EntP307 has been cloned under the control of the lambda PL promoter. This has enabled us to overproduce this protein and study its properties. Here we show that RepA1 is a soluble basic protein with an experimentally determined molecular weight of 40,000. Deletion analysis indicates that the overproduced protein originates from the open reading frame which we previously designated as coding for RepA1. We have also shown that the replication function of the replicon RepFIC depends on the intact RepA1 coding frame.
Maas
R
R
Department of Microbiology, New York University Medical Center, New York 10016.
Oppenheim
J
J
Saadi
S
S
Fuchs
T
T
Maas
W K
WK
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D001483:Base Sequence; D002872:Chromosome Deletion; D003001:Cloning, Molecular; D004252:DNA Mutational Analysis; D004261:DNA Replication / Q000235:genetics / Q000502:physiology; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics; D010957:Plasmids / Q000235:genetics*; D011401:Promoter Regions, Genetic / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D012093:Replicon / Q000235:genetics* / Q000502:physiology
D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; C070013:REPA1 protein, Bacteria