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Title
  • en Molecular cloning of MSSP-2, a c-myc gene single-strand binding protein: characterization of binding specificity and DNA replication activity.
Creator
Accessrights open access
Subject
  • MeSH en Base Sequence
  • MeSH en Cloning, Molecular
  • MeSH en Consensus Sequence
  • MeSH en DNA Primers/chemistry
  • MeSH en DNA Replication
  • MeSH en DNA, Complementary/genetics
  • MeSH en DNA-Binding Proteins/genetics
  • MeSH en DNA-Binding Proteins/metabolism
  • MeSH en Genes, myc
  • MeSH en Humans
  • MeSH en Molecular Sequence Data
  • MeSH en Mutagenesis, Site-Directed
  • MeSH en RNA-Binding Proteins
  • MeSH en Sequence Alignment
  • MeSH en Sequence Homology, Amino Acid
  • MeSH en Structure-Activity Relationship
  • NDC 499
Description
  • Abstract en We have previously reported the human cDNA encoding MSSP-1, a sequence-specific double- and single-stranded DNA binding protein [Negishi, Nishita, Saëgusa, Kakizaki, Galli, Kihara, Tamai, Miyajima, Iguchi-Ariga and Ariga (1994) Oncogene, 9, 1133-1143]. MSSP-1 binds to a DNA replication origin/transcriptional enhancer of the human c-myc gene and has turned out to be identical with Scr2, a human protein which complements the defect of cdc2 kinase in S.pombe [Kataoka and Nojima (1994) Nucleic Acid Res., 22, 2687-2693]. We have cloned the cDNA for MSSP-2, another member of the MSSP family of proteins. The MSSP-2 cDNA shares highly homologous sequences with MSSP-1 cDNA, except for the insertion of 48 bp coding 16 amino acids near the C-terminus. Like MSSP-1, MSSP-2 has RNP-1 consensus sequences. The results of the experiments using bacterially expressed MSSP-2, and its deletion mutants, as histidine fusion proteins suggested that the binding specificity of MSSP-2 to double- and single-stranded DNA is the same as that of MSSP-1, and that the RNP consensus sequences are required for the DNA binding of the protein. MSSP-2 stimulated the DNA replication of an SV40-derived plasmid containing the binding sequence for MSSP-1 or -2. MSSP-2 is hence suggested to play an important role in regulation of DNA replication.
Publisher en Oxford University Press
Date
    Issued1994-12-25
Language
  • eng
Resource Type journal article
Version Type VoR
Identifier HDL http://hdl.handle.net/2115/54041
Relation
  • isIdenticalTo DOI https://doi.org/10.1093/nar/22.25.5576
  • PMID 7838710
Journal
    • PISSN 0305-1048
      • en Nucleic acids research
      • Volume Number22 Issue Number25 Page Start5576 Page End5581
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Oaidate 2023-07-26