Difference between revisions of "Part:BBa K4395034"
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| + | SpyTag-UGT85A1-SpyCatcher is a fusion protein whose thermostability is increased by the SpyTag-SpyCatcher tagging system while the catalytic activity not affected. | ||
| + | The accumulation level of the trans-zeatin O-glucosides was significantly increased in UGT85A1 overexpressing transgenic Arabidopsis, while other forms of cytokinins kept the similar concentrations compared to the wild type. When treated with exogenously applied trans-zeatin, UGT85A1 overexpressing Arabidopsis showed much less sensitivity to trans-zeatin in primary root elongation and lateral root formation. It seems that overexpression of Arabidopsis glucosyltransferase UGT85A1 influences trans-zeatin homeostasis and trans-zeatin responses likely through O-glucosylation in planta.[1]These characteristics of UGT85A1 attract us and thus we choose it as one of the candidates UGTs of our experiment. | ||
| + | The SpyTag/SpyCatcher system is a split-in-two of the immunoglobulin-like collagen adhesion domain of Streptococcus pyogenes denoted CnaB2. CnaB2 is characterized by an internal isopeptide bond between residue Lys31 and residue Asp117. When split in two, one of which containing Lys31 and another containing Asp117, they associate and spontaneously form the isopeptide bond, thus join together [2] | ||
| + | The composite part SpyTag-UGT85A1-SpyCatcher is a fusion protein cyclized by the SpyTag/SpyCatcher system, whose two components are fused on both ends. This cyclization process increases the thermostability of the enzyme, enabling catalysis in an unfavored heated system [3]. | ||
| + | References: | ||
| + | [1] Jin S H, Ma X M, Kojima M, et al. Overexpression of glucosyltransferase UGT85A1 influences trans-zeatin homeostasis and trans-zeatin responses likely through O-glucosylation. Planta, 2013, 237: 991–999 [2] Long Li, Jacob O. Fierer, et al. Structural Analysis and Optimization of the Covalent Association between SpyCatcher and a Peptide Tag J Mol Biol. 2014 January 23; 426(2): 309–317 [3] Xiao-Bao Suna, Jia-Wen Caoa,b, et al. SpyTag/SpyCatcher molecular cyclization confers protein stability and resilience to aggregation | ||
Latest revision as of 07:18, 4 October 2022
SpyTag-UGT85A1-SpyCatcher is a fusion protein whose thermostability is increased by the SpyTag-SpyCatcher tagging system while the catalytic activity not affected. The accumulation level of the trans-zeatin O-glucosides was significantly increased in UGT85A1 overexpressing transgenic Arabidopsis, while other forms of cytokinins kept the similar concentrations compared to the wild type. When treated with exogenously applied trans-zeatin, UGT85A1 overexpressing Arabidopsis showed much less sensitivity to trans-zeatin in primary root elongation and lateral root formation. It seems that overexpression of Arabidopsis glucosyltransferase UGT85A1 influences trans-zeatin homeostasis and trans-zeatin responses likely through O-glucosylation in planta.[1]These characteristics of UGT85A1 attract us and thus we choose it as one of the candidates UGTs of our experiment. The SpyTag/SpyCatcher system is a split-in-two of the immunoglobulin-like collagen adhesion domain of Streptococcus pyogenes denoted CnaB2. CnaB2 is characterized by an internal isopeptide bond between residue Lys31 and residue Asp117. When split in two, one of which containing Lys31 and another containing Asp117, they associate and spontaneously form the isopeptide bond, thus join together [2] The composite part SpyTag-UGT85A1-SpyCatcher is a fusion protein cyclized by the SpyTag/SpyCatcher system, whose two components are fused on both ends. This cyclization process increases the thermostability of the enzyme, enabling catalysis in an unfavored heated system [3].
References: [1] Jin S H, Ma X M, Kojima M, et al. Overexpression of glucosyltransferase UGT85A1 influences trans-zeatin homeostasis and trans-zeatin responses likely through O-glucosylation. Planta, 2013, 237: 991–999 [2] Long Li, Jacob O. Fierer, et al. Structural Analysis and Optimization of the Covalent Association between SpyCatcher and a Peptide Tag J Mol Biol. 2014 January 23; 426(2): 309–317 [3] Xiao-Bao Suna, Jia-Wen Caoa,b, et al. SpyTag/SpyCatcher molecular cyclization confers protein stability and resilience to aggregation