Mutation of the small acidic tract A1 drastically reduces nucleoplasmin activity |
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Authors: | Salvany Lara Chiva Manel Arnan Carme Ausió Juan Subirana Juan A Saperas Núria |
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Affiliation: | Departament d'Enginyeria Química, ETSEIB, Universitat Politècnica de Catalunya, Diagonal 647, 08028 Barcelona, Spain. |
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Abstract: | Xenopus laevis nucleoplasmin is a molecular chaperone that mediates sperm decondensation and nucleosome assembly. Nucleoplasmin has three acidic tracts (A1, A2 and A3) and until recent years the long polyglutamic tract A2 was thought to be the binding site for basic proteins. However, the latest publications in this field show that neither A2 nor A3 is indispensable for histone and sperm-specific protein binding. In this work, we show that the mutation of only four acidic amino acid residues of the small A1 tract drastically reduces nucleoplasmin decondensing activity, pointing out this region as the potential binding site for sperm proteins. |
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Keywords: | r-NP, recombinant nucleoplasmin (-A1), mutation in the acidic tract A1 AU-PAGE, acetic acid-urea polyacrylamide gel electrophoresis SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis |
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