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1

Damaged DNA-binding proteins: recognition of N-acetoxyacetylaminofluorene-induced DNA adducts

100%
Rzeszowska-Wolny J., Widlak P.
Acta Biochimica Polonica
|
1999
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tom 46
|
nr 1
Proteins which bind to the DNA damaged by genotoxic agents can be detected in all living organisms. Damage-recognition proteins are thought to be generally involved in DNA repair mechanisms. On the other hand, the relevance to DNA repair of some other proteins which show elevated affinity to damaged DNA (e.g. HMG-box containing proteins or histone H1) has not been established. Using the electrophoretic mobility-shift assay we have investigated damage-recognition proteins in nuclei from rat hepatocytes. We detected two different protein complexes which preferentially bound the DNA damaged by N-acetoxy-acetylaminofluorene. One of them also recognized the DNA damaged by benzo(a)pyrene diol epoxide (yet with much lower efficiency). The proteins which bind to damaged DNA are permanently present in rat cells and their level does not change after treatment of animals with the carcinogens. Differences in the affinity of the detected damage-recognition proteins to DNA lesion evoked by either carcinogen did not correlate with more efficient removal from hepatic DNA of 2-acetylaminofluorene-induced adducts than benzo(a)pyrene-induced ones.
2

Brain-derived neurotrophic factor [BDNF]: role in neuronal development and survival

86%
Wozniak W.
Folia Morphologica
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1993
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tom 52
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nr 4
3

Detection of damage-recognition proteins from human lymphocytes

86%
Lanuszewska J., Cudak A., Rzeszowska-Wolny J., Widlak P.
Acta Biochimica Polonica
|
2000
|
tom 47
|
nr 2
Proteins recognizing and binding to damaged DNA (DDB-proteins) were analyzed in human lymphocytes obtained from healthy donors. Using an electrophoretic mobility shift assay several complexes between nuclear extract proteins and damaged DNA were detected: a complex specific for DNA damaged by N-acetoxy-N-acetylaminofluorene, another complex specific for UV-irradiated DNA, and two complexes specific for DNA damaged by cis-dichlorodiammine platinum. All the detected complexes differed in electrophoretic mobility and possibly contained different proteins. Complexes specific for free DNA ends were also detected in protein extracts from lymphocytes.
4

Detection and characterization of rat proteins recognizing and binding DNA damaged by N-acetoxyacetylaminofluorene and cis-platinum

86%
Pietrowska M., Lanuszewska J., Rzeszowska-Wolny J., Widlak P.
Cellular and Molecular Biology Letters
|
2000
|
tom 05
|
nr 2
5
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Ancient history of X-ray crystal structure of B-DNA oligomers and its perspective

58%
Grzeskowiak K., Ohishi H.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
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2011
|
tom 92
|
nr 3
6

Application of capillary electrophoresis for DNA-protein binding tests

58%
Kazmierczak A., Kazmierczak J. M.
Acta Physiologiae Plantarum
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2003
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tom 25
|
nr 1
7

Identification and properties of the Deinococcus grandis and Deinococcus proteolyticus single-stranded DNA binding proteins [SSB]

58%
Filipkowski P., Kur J.
Acta Biochimica Polonica
|
2007
|
tom 54
|
nr 1
To study the biochemical properties of SSB's from Deinococcus grandis (DgrSSB) and Deinococcus proteolyticus (DprSSB), we have cloned the ssb genes obtained by PCR and have developed Escherichia coli overexpression systems. The genes consist of an open reading frame of 891 (DgrSSB) and 876 (DprSSB) nucleotides encoding proteins of 296 and 291 amino acids with a calculated molecular mass of 32.29 and 31.33 kDa, respectively. The amino-acid sequence of DgrSSB exhibits 45%, 44% and 82% identity and the amino-acid sequence of DprSSB reveals 43%, 43% and 69% identity with Thermus aquaticus (TaqSSB), Thermus thermophilus (TthSSB) and Deinococcus radiodurans SSBs, respectively. We show that DgrSSB and DprSSB are similar to Thermus/Deinococcus SSBs in their biochemical properties. They are functional as homodimers, with each monomer encoding two single-stranded DNA binding domains (OB-folds). In fluorescence titrations with poly(dT), both proteins bind single-stranded DNA with a binding site size of about 33 nt per homodimer. In a complementation assay in E. coli, DgrSSB and DprSSB took over the in vivo function of EcoSSB. Thermostability with half-lives of about 1 min at 65-67.5°C make DgrSSB and DprSSB similar to the known SSB of Deinococcus radiodurans (DraSSB).
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