ArticleThe Biochemical journal1998
Evidence for the ability of nucleophosmin/B23 to bind ATP.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Review
- ATP:MgBiophysical journal · 2022Article
- A role for the CAL1-partner Modulo in centromere integrity and accurate chromosome segregation in Drosophila.PloS one · 2012Article
- The nuclear chaperone nucleophosmin escorts an Epstein-Barr Virus nuclear antigen to establish transcriptional cascades for latent infection in human B cells.PLoS pathogens · 2012Article
- Nucleophosmin and its complex network: a possible therapeutic target in hematological diseases.Oncogene · 2011Review
- NPM1/B23: A Multifunctional Chaperone in Ribosome Biogenesis and Chromatin Remodeling.Biochemistry research international · 2011Article
- Germline and somatic cancer-associated mutations in the ATP-binding motifs of PTEN influence its subcellular localization and tumor suppressive function.Human molecular genetics · 2009Article
- Article
- Conventional and nonconventional roles of the nucleolus.International review of cytology · 2002Review
- Nucleolar protein B23 has molecular chaperone activities.Protein science : a publication of the Protein Society · 1999Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
By taking advantage of its ability to be retained by ATP-agarose, we have demonstrated that nucleophosmin/B23 is capable of binding ATP. The specificity of the binding was confirmed by the absence of significant binding to AMP-agarose and by its loss when nucleophosmin/B23 in nuclear extracts was preincubated with ATP. Preincubation of the nuclear extracts with other ribonucleotide triphosphates (GTP, CTP, UTP) did not compete for the binding of nucleophosmin/B23 to ATP-agarose. The purified recombinant nucleophosmin/B23 was also able to be retained by ATP-agarose. The Kd for binding of ATP to the purified recombinant nucleophosmin/B23, on the basis of retention on a nitrocellulose membrane, was 86.5+/-8.3 microM; the number of binding sites was 0.68 per nucleophosmin/B23 protein molecule. To determine the possible ATP-binding site of nucleophosmin/B23, various deletion clones including the two mutants in which the putative ATP-binding sequence had been deleted were constructed. Deletion of the portions of the molecule (residues 83-152 and 185-240) had little effect on the ATP binding. The C-terminal deleted mutant (residue 242 to the C-terminus deleted) lost most of its ability to be retained by ATP-agarose and to bind [alpha-32P]ATP on a nitrocellulose membrane. The results indicate that the C-terminal portion (residues 242-294) contains the essential ATP-binding site of nucleophosmin/B23.
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