Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 360, Issue 3, Pages 548-557Publisher
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.05.048
Keywords
human pancreatic ribonuclease; NLS; importin alpha; molecular recognition; protein-protein interactions
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Nuclear import of proteins is determined by specific signals that allow them to bind to receptors that mediate their energy-dependent transport through the nuclear pore. These signals are termed nuclear localization signals and do not constitute a specific consensus sequence. Among them, the most characterized correspond to monopartite and bipartite nuclear localization signals, which interact with the importin alpha/beta heterodimer. We previously described a cytotoxic variant of human pancreatic-ribonuclease that is actively transported into the nucleus. Here, we show that this protein interacts with importin alpha through different basic residues, including Lysl and the arginine clusters 31-33 and 89-91. Although these residues are scattered along the sequence, they are close in the three-dimensional structure of the protein and their topological disposition strongly resembles that of a classical bipartite nuclear localization signal. (c) 2006 Elsevier Ltd. All rights reserved.
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