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Thakur J.K.,National Institute of Plant Genome Research Aruna Asaf Ali Marg | Agarwal P.,National Institute of Plant Genome Research Aruna Asaf Ali Marg | Parida S.,National Institute of Plant Genome Research Aruna Asaf Ali Marg | Bajaj D.,National Institute of Plant Genome Research Aruna Asaf Ali Marg | Pasrija R.,National Institute of Plant Genome Research Aruna Asaf Ali Marg
Molecular Genetics and Genomics | Year: 2013

The KIX domain, which mediates protein-protein interactions, was first discovered as a motif in the large multidomain transcriptional activator histone acetyltransferase p300/CBP. Later, the domain was also found in Mediator subunit MED15, where it interacts with many transcription factors. In both proteins, the KIX domain is a target of activation domains of diverse transcription activators. It was found to be an essential component of several specific gene-activation pathways in fungi and metazoans. Not much is known about KIX domain proteins in plants. This study aims to characterize all the KIX domain proteins encoded by the genomes of Arabidopsis and rice. All identified KIX domain proteins are presented, together with their chromosomal locations, phylogenetic analysis, expression and SNP analyses. KIX domains were found not only in p300/CBP- and MED15-like plant proteins, but also in F-box proteins in rice and DNA helicase in Arabidopsis, suggesting roles of KIX domains in ubiquitin-mediated proteasomal degradation and genome stability. Expression analysis revealed overlapping expression of OsKIX-3, OsKIX-5 and OsKIX-7 in different stages of rice seeds development. Moreover, an association analysis of 136 in silico mined SNP loci in 23 different rice genotypes with grain-length information identified three non-synonymous SNP loci in these three rice genes showing strong association with long- and short-grain differentiation. Interestingly, these SNPs were located within KIX domain encoding sequences. Overall, this study lays a foundation for functional analysis of KIX domain proteins in plants. © 2013 Springer-Verlag Berlin Heidelberg.

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