+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Purification and characterization of a protein from Escherichia coli which forms complexes with superhelical and single-stranded DNAs



Purification and characterization of a protein from Escherichia coli which forms complexes with superhelical and single-stranded DNAs



Journal of Biochemistry 92(4): 1059-1068



From the cells of an Escherichia coli K-12 strain, a 22,000-dalton protein which has an affinity for the superhelical DNA molecule was purified to apparent homogeneity by monitoring the DNA-binding activity using the filter binding assay. In the sedimentation analysis of the DNA-protein complex, the protein has an affinity for the superhelical or single-stranded DNA molecule but neither for the open-circular nor for the linear DNA molecule. The amino acid composition of the protein resembled those of the other prokaryotic histone-like proteins and also to eukaryotic histones H2A and H2B. The protein precipitated upon heating, which is in contrast to the heat-stable feature of the other histone-like proteins. Furthermore, DNA and RNA syntheses in vitro were not affected by the presence of the protein. In view of these characteristics, this protein may play a role in maintaining the bacterial nucleoid structure.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 044102087

Download citation: RISBibTeXText

PMID: 6294066


Related references

Purification and Characterization of a Protein from Escherichia coli which Forms Complexes with Superhelical and Single-Stranded Dnas. The Journal of Biochemistry 92(4): 1059-1068, 1982

Purification and characterization of a protein from escherichia coli which complexes with super helical and single stranded dna species. Journal of Biochemistry 92(4): 1059-1068, 1982

Homologous pairing of single-stranded DNA and superhelical double-stranded DNA catalyzed by RecO protein from Escherichia coli. Journal of Bacteriology 177(3): 566-572, 1995

Escherichia coli single-strand binding protein forms multiple, distinct complexes with single-stranded DNA. Biochemistry 25(24): 7799-7802, 1986

Escherichia coli ssb protein forms multiple distinct complexes with single stranded dna. Biophysical Journal 51(2 PART 2): 149A, 1987

Continuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA. Biochemistry 25(7): 1482-1494, 1986

Purification and characterization of the Escherichia coli RecO protein. Renaturation of complementary single-stranded DNA molecules catalyzed by the RecO protein. Journal of Molecular Biology 236(1): 124-138, 1994

Effects of escherichia coli ssb protein on the single stranded dna dependent atpase activity of escherichia coli reca protein evidence that ssb protein facilitates the binding of reca protein to regions of secondary structure within single stranded dna. Journal of Molecular Biology 193(1): 97-114, 1987

C-terminal truncated Escherichia coli RecA protein RecA5327 has enhanced binding affinities to single- and double-stranded DNAs. Journal of Molecular Biology 223(1): 115-129, 1992

Effect of polyethylene glycol on transfection of Escherichia coli spheroplasts with bacteriophage .Phi.X174 single-stranded and double-stranded Dnas. Agricultural and Biological Chemistry 41(3): 567-571, 1977

Stabilization of recA protein-ssDNA complexes by the single-stranded DNA binding protein of Escherichia coli. Biochemistry 29(3): 837-843, 1990

Stable complexes between escherichia coli protein omega and single or double stranded dna. Federation Proceedings 35(7): 684, 1976

The purification from Escherichia coli of a protein relaxing superhelical DNA. Canadian Journal of Biochemistry 54(4): 301-306, 1976

Novel crystal forms of a proteolytic core of the single stranded dna binding protein from escherichia coli. Febs Letters 170(1): 143-146, 1984

Triplet state properties of tryptophan residues in complexes of mutated Escherichia coli single-stranded DNA binding proteins with single-stranded polynucleotides. Biophysical Journal 55(5): 927-936, 1989