Mapping the native interaction surfaces of PREP1 with PBX1 by cross-linking mass-spectrometry and mutagenesis(15 views visite) Bruckmann C, Tamburri S, De Lorenzi V, Doti N, Monti A, Mathiasen L, Cattaneo A, Ruvo M, Bachi A, Blasi F
Sci Rep (ISSN: 2045-2322linking), 2020 Oct 8; 10(1): 16809-16809.
Keywords Parole chiave: A549 Cells, Binding Sites, Cloning, Molecular, Enzyme-Linked Immunosorbent Assay, Homeodomain Proteins Metabolism, Humans, Mass Spectrometry, Mutagenesis, Myeloid Ecotropic Viral Integration Site 1 Protein Metabolism, Pre-B-Cell Leukemia Transcription Factor 1 Metabolism, Protein Interaction Mapping Methods
Affiliations Affiliazioni: *** IBB - CNR ***
IFOM (Foundation FIRC Institute of Molecular Oncology), Via Adamello 16, 20139, Milan, Italy. chiara.bruckmann@ifom.eu.
Department of Experimental Oncology, European Institute of Oncology, Via Adamello 16, 20139, Milan, Italy.
Center for Nanotechnology Innovation@NEST, Istituto Italiano di Tecnologia, Piazza San Silvestro 12, 56124, Pisa, Italy.
Institute of Biostructures and Bioimaging (IBB)-CNR, Via Mezzocannone 16, 80134, Naples, Italy.
Cogentech S.R.L. Benefit Corporation IT, Via Adamello 16, 20139, Milan, Italy.
References Riferimenti: Not available. Non disponibili.
Mapping the native interaction surfaces of PREP1 with PBX1 by cross-linking mass-spectrometry and mutagenesis
Both onco-suppressor PREP1 and the oncogene MEIS1 bind to PBX1. This interaction stabilizes the two proteins and allows their translocation into the nucleus and thus their transcriptional activity. Here, we have combined cross-linking mass-spectrometry and systematic mutagenesis to detail the binding geometry of the PBX1-PREP1 (and PBX1-MEIS1) complexes, under native in vivo conditions. The data confirm the existence of two distinct interaction sites within the PBC domain of PBX1 and unravel differences among the highly similar binding sites of MEIS1 and PREP1. The HR2 domain has a fundamental role in binding the PBC-B domain of PBX1 in both PREP1 and MEIS1. The HR1 domain of MEIS1, however, seem to play a less stringent role in PBX1 interaction with respect to that of PREP1. This difference is also reflected by the different binding affinity of the two proteins to PBX1. Although partial, this analysis provides for the first time some ideas on the tertiary structure of the complexes not available before. Moreover, the extensive mutagenic analysis of PREP1 identifies the role of individual hydrophobic HR1 and HR2 residues, both in vitro and in vivo.
Mapping the native interaction surfaces of PREP1 with PBX1 by cross-linking mass-spectrometry and mutagenesis
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