The distribution of different classes of nuclear localization signals (NLSs) in diverse organisms and the utilization of the minor NLS-binding site in plant nuclear import factor importin-α

Chiung Wen Chang, Rafael Miguez Couñago, Simon J. Williams, Mikael Boden, Bostjan Kobe*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

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 languageEnglish
JournalPlant Signaling and Behavior
Volume8
Issue number10
DOIs
Publication statusPublished - Oct 2013
Externally publishedYes

Fingerprint

Dive into the research topics of 'The distribution of different classes of nuclear localization signals (NLSs) in diverse organisms and the utilization of the minor NLS-binding site in plant nuclear import factor importin-α'. Together they form a unique fingerprint.

Cite this