Sequence and expression analyses of KIX domain proteins suggest their importance in seed development and determination of seed size in rice, and genome stability in Arabidopsis
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Title |
Sequence and expression analyses of KIX domain proteins suggest their importance in seed development and determination of seed size in rice, and genome stability in Arabidopsis
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Creator |
Thakur, Jitendra K.
Agarwal, Pinky Parida, Swarup K. Bajaj, Deepak Pasrija, Richa |
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Subject |
KIX domain
Mediator MED15 p300/CBP Rice Arabidopsis |
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Description |
Accepted date: 17 May 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. This work was supported by IYBA Grant (BT/ BI/12/045/2008) from the Department of Biotechnology, Ministry of Science and Technology, Government of India, to JKT. We thank Professor AK Tyagi for his valuable comments on the manuscript. We acknowledge Dr. Stefan Oehler for his important suggestions and editing the MS. |
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Date |
2015-11-24T09:45:12Z
2015-11-24T09:45:12Z 2013 |
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Type |
Article
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Identifier |
Mol. Genet. Genomics, 288(7-8): 329-346
1617-4623 http://172.16.0.77:8080/jspui/handle/123456789/377 http://link.springer.com/article/10.1007%2Fs00438-013-0753-9 10.1007/s00438-013-0753-9 |
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Language |
en_US
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Publisher |
Springer
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