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PMID:8643677

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Citation

Borden, KL, Lally, JM, Martin, SR, O'Reilly, NJ, Solomon, E and Freemont, PS (1996) In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML. Proc. Natl. Acad. Sci. U.S.A. 93:1601-6

Abstract

Acute promyelocytic leukemia (APL) has been ascribed to a chromosomal translocation event which results in a fusion protein comprising the PML protein and retinoic acid receptor alpha. PML is normally a component of a nuclear multiprotein complex which is disrupted in the APL disease state. Here, two newly defined cysteine/histidine-rich protein motifs called the B-box (B1 and B2) from PML have been characterized in terms of their effect on PML nuclear body formation, their dimerization, and their biophysical properties. We have shown that both peptides bind Zn2+, which induces changes in the peptides' structures. We demonstrate that mutants in both B1 and B2 do not form PML nuclear bodies in vivo and have a phenotype that is different from that observed in the APL disease state. Interestingly, these mutations do not affect the ability of wild-type PML to dimerize with mutant proteins in vitro, suggesting that the B1 and B2 domains are involved in an additional interaction central to PML nuclear body formation. This report in conjunction with our previous work demonstrates that the PML RING-Bl/B2 motif plays a fundamental role in formation of a large multiprotein complex, a function that may be common to those unrelated proteins which contain the motif.

Links

PubMed PMC39988

Keywords

Allosteric Site; Amino Acid Sequence; Binding Sites; Cobalt/metabolism; Histidine; Humans; Leukemia, Promyelocytic, Acute/metabolism; Ligands; Molecular Sequence Data; Mutagenesis, Site-Directed; Neoplasm Proteins/chemistry; Neoplasm Proteins/genetics; Neoplasm Proteins/metabolism; Nuclear Proteins; Oncogene Proteins, Fusion/chemistry; Oncogene Proteins, Fusion/genetics; Oncogene Proteins, Fusion/metabolism; Peptide Fragments/chemistry; Protein Conformation; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Transcription Factors/chemistry; Transcription Factors/metabolism; Transfection; Tumor Suppressor Proteins; Zinc/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:PML

involved_in

GO:0030578: PML body organization

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete


See also

References

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