Abstract
The specific recognition between the import receptor importin-α and the nuclear localization signals (NLSs) is crucial to ensure the selective transport of cargoes into the nucleus. NLSs contain one or two clusters of positively-charged amino-acids, which usually bind to the major (monopartite NLSs) or both minor and major NLS-binding sites (bipartite NLSs). In our recent study, we determined the structure of importin-α1a from rice (Oryza sativa), and made two observations that suggest an increased utilization of the minor NLS-binding site in this protein. First, unlike the mammalian protein, both the major and minor NLS-binding sites are auto-inhibited in the unliganded rice protein. Second, we showed that NLSs of the 'plant-specific' class preferentially bind to the minor NLS-binding site of rice importin-α. Here, we show that a distinct group of 'minor site-specific' NLSs also bind to the minor site of the rice protein. We further show a greater enrichment of proteins containing these plant-specific' and 'minor site-specific' NLSs in the rice proteome. However, the analysis of the distribution of different classes of NLSs in diverse eukaryotes shows that in all organisms, the minor site-specific NLSs are much less prevalent than the classical monopartite and bipartite NLSs.
| Original language | English |
|---|---|
| Journal | Plant Signaling and Behavior |
| Volume | 8 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - Oct 2013 |
| Externally published | Yes |
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