Abstract
The ubiquitin proteasome 26S system (UPS), involving monomeric and multimeric E3 ligases is one of the most important signaling pathways in many organisms, including plants. The SCF (SKP1/Cullin/F-box) multimeric complex is particularly involved in response to development and stress signaling. The SKP1 protein (S-phase kinase-associated protein 1) is the core subunit of this complex. In this work, we firstly identified 92 and 87 non-redundant Triticum aestivum SKP1-like (TaSKP) genes that were retrieved from the latest release of the wheat genome database (International Wheat Genome Sequencing Consortium (IWGSC) RefSeq v1.0) and the genome annotation of the TGAC v1 respectively. We then investigated the structure, phylogeny, duplication events and expression patterns of the SKP1-like gene family in various tissues and environmental conditions using a wheat expression platform containing public data. TaSKP1-like genes were expressed differentially in response to stress conditions, displaying large genomic variations or short insertions/deletions which suggests functional specialization within TaSKP1-like genes. Finally, interactions between selected wheat FBX (F-box) proteins and putative ancestral TaSKP1-like proteins were tested using the yeast two-hybrid (Y2H) system to examine the molecular interactions. These observations suggested that six Ta-SKP1 genes are likely to be ancestral genes, having similar functions as ASK1 and ASK2 in Arabidopsis, OSK1 and OSK20 in rice and PpSKP1 and PpSKP2 in Physcomitrella patens.
Highlights
IntroductionSelective degradation of proteins plays a key role in diverse aspects of eukaryotic mechanisms such as responses to physiological development (flowering, cell cycle, etc.) or in responses to diverse environmental stresses [1,2,3,4,5,6] by degrading target proteins that play a role in the activation or repression of downstream genes
Selective degradation of proteins plays a key role in diverse aspects of eukaryotic mechanisms such as responses to physiological development or in responses to diverse environmental stresses [1,2,3,4,5,6] by degrading target proteins that play a role in the activation or repression of downstream genes
HMMER2-BLASTP-InterProScan searches of databases containing the latest version of the annotated wheat genome database (International Wheat Genome Sequencing Consortium (IWGSC RefSeq v1.0)) and in TGAC v1 [28] identified 92 and 87 non-redundant Triticum aestivum SKP1-like genes, respectively, with conserved Skp1 and Skp1_POZ (POxvirus and Zinc finger) domains
Summary
Selective degradation of proteins plays a key role in diverse aspects of eukaryotic mechanisms such as responses to physiological development (flowering, cell cycle, etc.) or in responses to diverse environmental stresses [1,2,3,4,5,6] by degrading target proteins that play a role in the activation or repression of downstream genes. The substrate selectivity is insured by E3 ubiquitin ligases which could be monoor multi-subunit complexes. Among the multi-subunit E3 ubiquitin ligases complexes, the SKP1/Cullin 1/F-box protein (SCF) family is well characterized [7,8]. Each SCF complex is composed of four protein components: the Cul1-Rbx (Cullin 1/ RING-box protein 1) catalytic core bound to a variable F-box protein (FBX)-Skp substrate recognition module [9,10]. SKP1 is a small protein of approximately 160 amino acids and functions as a core component connecting CUL1 and an F-box protein. SKP1 plays crucial roles in cell-cycle progression, in hormone and light signaling [11,12,13,14,15,16] as well as in vegetative and flower development [17,18,19,20,21]
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