ArticleProceedings of the National Academy of Sciences of the United States of America1996
Mutational analysis of NM23-H2/NDP kinase identifies the structural domains critical to recognition of a c-myc regulatory element.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 76 citations in OpenAlex.
- Mutations at the dimer interface and surface residues of Nm23-H1 metastasis suppressor affect its expression and function.Molecular and cellular biochemistry · 2020Article
- Characterization of Nme5-Like Gene/Protein from the Red AlgaMarine drugs · 2019Article
- Article
- Nuclear functions of NME proteins.Laboratory investigation; a journal of technical methods and pathology · 2018Review
- NM23/NDPK proteins in transcription regulatory functions and chromatin modulation: emerging trends.Laboratory investigation; a journal of technical methods and pathology · 2018Review
- Epigenetic suppression of human telomerase (The Journal of biological chemistry · 2017Article
- Chemical intervention of the NM23-H2 transcriptional programme on c-MYC via a novel small molecule.Nucleic acids research · 2015Article
- Regulatory functions of Nm23-H2 in tumorigenesis: insights from biochemical to clinical perspectives.Naunyn-Schmiedeberg's archives of pharmacology · 2015Review
- NDK-1, the homolog of NM23-H1/H2 regulates cell migration and apoptotic engulfment in C. elegans.PloS one · 2014Article
- A critical evaluation of biochemical activities reported for the nucleoside diphosphate kinase/Nm23/Awd family proteins: opportunities and missteps in understanding their biological functions.Naunyn-Schmiedeberg's archives of pharmacology · 2011Article
- DENN domain proteins: regulators of Rab GTPases.The Journal of biological chemistry · 2011Review
- Metastasis suppressor function of NM23-H1 requires its 3'-5' exonuclease activity.International journal of cancer · 2011Article
- NM23-H2 may play an indirect role in transcriptional activation of c-myc gene expression but does not cleave the nuclease hypersensitive element III(1).Molecular cancer therapeutics · 2009Article
- Xenopus NM23-X4 regulates retinal gliogenesis through interaction with p27Xic1.Neural development · 2009Article
- Metastases suppressor NM23-H2 interaction with G-quadruplex DNA within c-MYC promoter nuclease hypersensitive element induces c-MYC expression.Nucleic acids research · 2009Article
- The trypanosome transcriptome is remodelled during differentiation but displays limited responsiveness within life stages.BMC genomics · 2008Article
- Multiple biochemical activities of NM23/NDP kinase in gene regulation.Journal of bioenergetics and biomembranes · 2003Review
- New insights into Nm23 control of cell adhesion and migration.Journal of bioenergetics and biomembranes · 2003Review
- Normal transcription of the C1 inhibitor gene is dependent upon a polypurine-polypyrimidine region within the promoter.Inflammation · 2002Article
- Catalysis of DNA cleavage and nucleoside triphosphate synthesis by NM23-H2/NDP kinase share an active site that implies a DNA repair function.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
NM23-H2, a presumed regulator of tumor metastasis in humans, is a hexameric protein with both enzymatic (NDP kinase) and regulatory (transcriptional activation) activity. While the structure and catalytic mechanisms have been well characterized, the mode of DNA binding is not known. We examined this latter function in a site-directed mutational study and identified residues and domains essential for the recognition of a c-myc regulatory sequence. Three amino acids, Arg-34, Asn-69, and Lys-135, were found among 30 possibilities to be critical for DNA binding. Two of these, Asn-69 and Lys-135, are not conserved between NM23 variants differing in DNA-binding potential, suggesting that DNA recognition resides partly in nonconserved amino acids. All three DNA-binding defective mutant proteins are active enzymatically and appear to be stable hexamers, suggesting that they perform at the level of DNA recognition and that separate functional domains exist for enzyme catalysis and DNA binding. In the context of the known crystal structure of NM23-H2, the DNA-binding residues are located within distinct structural motifs in the monomer, which are exposed to the surface near the 2-fold axis of adjacent subunits in the hexamer. These findings are explained by a model in which NM23-H2 binds DNA with a combinatorial surface consisting of the "outer" face of the dimer. Chemical crosslinking data support a dimeric DNA-binding mode by NM23-H2.
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