000124072 001__ 124072
000124072 005__ 20240319081030.0
000124072 0247_ $$2doi$$a10.3390/ijms232315333
000124072 0248_ $$2sideral$$a132578
000124072 037__ $$aART-2022-132578
000124072 041__ $$aeng
000124072 100__ $$aRizzuti, Bruno
000124072 245__ $$aDeciphering the Binding of the Nuclear Localization Sequence of Myc Protein to the Nuclear Carrier Importin a3
000124072 260__ $$c2022
000124072 5060_ $$aAccess copy available to the general public$$fUnrestricted
000124072 5203_ $$aThe oncoprotein Myc is a transcription factor regulating global gene expression and modulating cell proliferation, apoptosis, and metabolism. Myc has a nuclear localization sequence (NLS) comprising residues Pro320 to Asp328, to allow for nuclear translocation. We designed a peptide comprising such region and the flanking residues (Ala310-Asn339), NLS-Myc, to study, in vitro and in silico, the ability to bind importin α3 (Impα3) and its truncated species (ΔImpα3) depleted of the importin binding domain (IBB), by using fluorescence, circular dichroism (CD), biolayer interferometry (BLI), nuclear magnetic resonance (NMR), and molecular simulations. NLS-Myc interacted with both importin species, with affinity constants of ~0.5 µM (for Impα3) and ~60 nM (for ΔImpα3), as measured by BLI. The molecular simulations predicted that the anchoring of NLS-Myc took place in the major binding site of Impα3 for the NLS of cargo proteins. Besides clarifying the conformational behavior of the isolated NLS of Myc in solution, our results identified some unique properties in the binding of this localization sequence to the nuclear carrier Impα3, such as a difference in the kinetics of its release mechanism depending on the presence or absence of the IBB domain.
000124072 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000124072 590__ $$a5.6$$b2022
000124072 592__ $$a1.154$$b2022
000124072 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b66 / 285 = 0.232$$c2022$$dQ1$$eT1
000124072 593__ $$aMedicine (miscellaneous)$$c2022$$dQ1
000124072 591__ $$aCHEMISTRY, MULTIDISCIPLINARY$$b52 / 178 = 0.292$$c2022$$dQ2$$eT1
000124072 593__ $$aPhysical and Theoretical Chemistry$$c2022$$dQ1
000124072 593__ $$aComputer Science Applications$$c2022$$dQ1
000124072 593__ $$aInorganic Chemistry$$c2022$$dQ1
000124072 593__ $$aSpectroscopy$$c2022$$dQ1
000124072 593__ $$aOrganic Chemistry$$c2022$$dQ1
000124072 593__ $$aMolecular Biology$$c2022$$dQ2
000124072 593__ $$aCatalysis$$c2022$$dQ2
000124072 594__ $$a7.8$$b2022
000124072 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000124072 700__ $$aIovanna, Juan L.
000124072 700__ $$aNeira, José L.
000124072 773__ $$g23, 23 (2022), 15333 [19 pp.]$$pInt. j. mol. sci.$$tInternational Journal of Molecular Sciences$$x1661-6596
000124072 8564_ $$s3098094$$uhttps://zaguan.unizar.es/record/124072/files/texto_completo.pdf$$yVersión publicada
000124072 8564_ $$s2664608$$uhttps://zaguan.unizar.es/record/124072/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000124072 909CO $$ooai:zaguan.unizar.es:124072$$particulos$$pdriver
000124072 951__ $$a2024-03-18-17:05:21
000124072 980__ $$aARTICLE