Abstract
Small ubiquitin-like modifier (SUMO) modification (SUMOylation) is an important and widely used reversible modification system in eukaryotic cells. It regulates various cell processes, including protein targeting, transcriptional regulation, signal transduction, and cell division. To understand its role in the model lepidoptera insect Bombyx mori, a recombinant baculovirus was constructed to express an enhanced green fluorescent protein (eGFP)-SUMO fusion protein along with ubiquitin carrier protein 9 of Bombyx mori (BmUBC9). SUMOylation substrates from Bombyx mori cells infected with this baculovirus were isolated by immunoprecipitation and identified by LC–ESI-MS/MS. A total of 68 candidate SUMOylated proteins were identified, of which 59 proteins were functionally categorized to gene ontology (GO) terms. Analysis of kyoto encyclopedia of genes and genomes (KEGG) pathways showed that 46 of the identified proteins were involved in 76 pathways that mainly play a role in metabolism, spliceosome and ribosome functions, and in RNA transport. Furthermore, SUMOylation of four candidates (polyubiquitin-C-like isoform X1, 3-hydroxyacyl-CoA dehydrogenase, cyclin-related protein FAM58A-like and GTP-binding nuclear protein Ran) were verified by co-immunoprecipitation in Drosophila schneide 2 cells. In addition, 74% of the identified proteins were predicted to have at least one SUMOylation site. The data presented here shed light on the crucial process of protein sumoylation in Bombyx mori.
Highlights
Post-translational modifications (PTMs) involve the addition of a chemical group to the protein after it has been generated by the translational machinery
It has been reported that in the HeLa cell line, Small ubiquitin-like modifier (SUMO)-1, SUMO-2, and SUMO-3 proteins are all localized in the nuclear membrane, in the nuclear bodies, and in the cytoplasm [4,21]
Fluorescence was observed across the entire cell, it was mainly observed in the cytoplasm and appeared as aggregated dots in the nucleus (Figure 1). The latter observation was in accordance with that of a previous study that found that many SUMOylated proteins are located in the nucleus [22]
Summary
Post-translational modifications (PTMs) involve the addition of a chemical group to the protein after it has been generated by the translational machinery. PTMs are essential for a variety of cellular processes and provide an important type of post-translational regulation. Processes such as transcriptional regulation [5] and protein degradation [6]. Small ubiquitin-like modifier (SUMO) modification (SUMOylation), another type of PTM, is structurally related to ubiquitin. The 3-D structure of the human small ubiquitin-like modifier 1 (SUMO-1). Protein is very similar to that of ubiquitin and in several instances SUMO competes with ubiquitin for a given lysine acceptor site, thereby preventing its subsequent poly-ubiquitination and degradation by the proteasome [7,8]. SUMO is believed to play roles in various cellular processes, including protein interaction, subcellular localization, and transcriptional regulation [9,10]
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