title: The Arabidopsis thaliana apurinic endonuclease Arp reduces human transcription factors Fos and Jun.
abstract: An Arabidopsis thaliana cDNA encoding an analogue, referred to as Arp for apurinic endonuclease-redox protein, of the human redox factor REF has been cloned. Arp stimulates in vitro DNA-binding activity of the human transcription factor Jun and Fos by the reduction of a cysteine residue located in the DNA-binding domain. Based on amino acid sequence homology, this redox activity is probably confined to the small internal domain of the Arp protein. In analogy to REF, we show that the Arabidopsis Arp protein also functions as an apurinic/apyrimidinic class II endonuclease. This base-free endonuclease activity resides in the carboxyl-terminal domain, and this part of the protein has significant sequence similarity to bacterial (Escherichia coli exonuclease III and Streptococcus pneumoniae exonuclease A) and animal (Drosophila Rrp1 and human REF/HAP) apurinic/apyrimidinic endonucleases. The amino-terminal domain of the Arp protein is highly charged and apparently increases the affinity of the protein for DNA. Therefore, the Arabidopsis Arp protein is multifunctional and may be involved both in DNA repair and in the regulation of transcription.
authors.affiliation: Laboratorium voor Genetica, Universiteit Gent, Belgium.
authors.forename: E
authors.initials: E
authors.lastname: Babiychuk
authors.forename: S
authors.initials: S
authors.lastname: Kushnir
authors.forename: M
authors.initials: M
authors.lastname: Van Montagu
authors.forename: D
authors.initials: D
authors.lastname: Inzé
mesh_terms: D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular; D017931:DNA Primers / Q000737:chemistry; D018076:DNA, Complementary / Q000235:genetics; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase; D043223:Deoxyribonuclease IV (Phage T4-Induced); D004706:Endodeoxyribonucleases / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D017343:Genes, Plant; D006801:Humans; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D016755:Proto-Oncogene Proteins c-jun / Q000378:metabolism*; D011994:Recombinant Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D017931:DNA Primers; D018076:DNA, Complementary; D029968:Escherichia coli Proteins; D016755:Proto-Oncogene Proteins c-jun; D011994:Recombinant Proteins; D004706:Endodeoxyribonucleases; D043223:Deoxyribonuclease IV (Phage T4-Induced); C468972:endonuclease IV, E coli; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase