PROPERTIES OF A SINGLE-STRAND DNA BINDING PROTEIN FROM RAT LIVER

1981 ◽  
Vol 9 (2) ◽  
pp. 128P-128P
Author(s):  
C. BONNE ◽  
M. DUGUET ◽  
A-M de RECONDO
Keyword(s):  
Dna Binding ◽  
Rat Liver ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Strand

scholarly journals Purification and general properties of the DNA-binding protein (P16) from rat liver mitochondria.

1985 ◽  
Vol 100 (1) ◽  
pp. 258-264 ◽  
Author(s):  
P A Pavco ◽  
G C Van Tuyle
Keyword(s):  
Mitochondrial Dna ◽  
Dna Binding ◽  
Rat Liver ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Liver Mitochondria ◽  
Single Strand ◽  
Proteinase K ◽  
Rat Liver Mitochondria

The mitochondrial DNA-binding protein P16 was isolated from rat liver mitochondrial lysates by affinity chromatography on single strand DNA agarose and separated from DNA in the preparation by alkaline CsCl isopycnic gradients. The top fraction of the gradients contained a single polypeptide species (Mr approximately equal to 15,200) based upon SDS PAGE. Digestion of single strand DNA-bound P16 with proteinase K produced a protease-insensitive, DNA-binding fragment (Mr approximately equal to 6,000) that has been purified by essentially the same procedures used for intact P16. The partial amino acid compositions for P16 and the DNA-binding fragment were obtained by conventional methods. Analysis of subcellular fractions revealed that nearly all of the cellular P16 was located in the mitochondria and that only trace amounts of protein of comparable electrophoretic mobility could be isolated from the nuclear or cytoplasmic fractions. The labeling of P16 with [35S]methionine in primary rat hepatocyte cultures was inhibited by more than 90% by the cytoplasmic translation inhibitor cycloheximide, but unaffected by the mitochondrial-specific agent chloramphenicol. These results indicate that P16 is synthesized on cytoplasmic ribosomes and imported into the mitochondria. The addition of purified P16 to deproteinized mitochondrial DNA resulted in the complete protection of the labeled nascent strands of displacement loops against branch migrational loss during cleavage of parental DNA with SstI, thus providing strong evidence that P16 is the single entity required for this in vitro function. Incubation of P16 with single strand phi X174 DNA, double strand (RF) phi X174 DNA, or Escherichia coli ribosomal RNA and subsequent analysis of the nucleic acid species for bound protein indicated a strong preference of P16 for single strand DNA and no detectable affinity for RNA or double strand DNA. Examination of P16-single strand phi X174 DNA complexes by direct electron microscopy revealed thickened, irregular fibers characteristic of protein-associated single strand DNA.

scholarly journals Single-strand DNA binding protein from rat liver: interactions with supercoiled DNA

1980 ◽  
Vol 8 (21) ◽  
pp. 4955-4968 ◽  
Author(s):  
Catherine Bonne ◽  
Michel Duguet ◽  
Anne-Marie de Recondo
Keyword(s):  
Dna Binding ◽  
Rat Liver ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Strand ◽  
Supercoiled Dna

Characterization of an adenovirus early protein required for viral DNA replication: A single strand specific DNA binding protein

1976 ◽  
Vol 11 (2) ◽  
pp. 79-95 ◽  
Author(s):  
A. J. Levine ◽  
P. C. van der Vliet ◽  
B. Rosenwirth ◽  
C. Anderson ◽  
J. Rabek ◽  
...  
Keyword(s):  
Dna Replication ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Strand ◽  
Viral Dna ◽  
Viral Dna Replication ◽  
Early Protein

Post-ultraviolet DNA Synthesis in the Absence of Repair: Role of the Single-strand DNA-binding Protein

1989 ◽  
Vol 55 (5) ◽  
pp. 739-745 ◽  
Author(s):  
Ž. Trgovčević ◽  
N. Lerš ◽  
K. Brčić-Kostić ◽  
E. Salaj-Šmic
Keyword(s):  
Dna Binding ◽  
Dna Synthesis ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Strand
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