Відмінності між версіями «THYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN-LIKE two (EGY2) UBIQUITIN-SPECIFIC PROTEASE 5 (UBP5) UBIQUITIN-SPECIFIC PROTEASE 6 (UBP»
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| − | + | Within the [http://hs21.cn/comment/html/?201370.html Ess, 2010); I. McLean, The Legend of Red Clydeside (Edinburgh, Scotland: John] absence of ASK1, the accumulation of those transcriptional repressors or activators benefits in down-regulation or upregulation of gene transcription, respectively. Ribosomal proteins could share a similar mechanism: accumulation of ribosomal proteins in ask1 might improve protein synthesis; alternatively, if ribosomal proteins have extraribosomal regulatory functions, they may stabilize some proteins in a related way as these stabilizing p53 in human [67]. In a further attainable situation, ASK1-E3s may well destabilize some proteolytic enzymes (e.g., E3 ubiquitin ligases orLu et al. BMC Plant Biology (2016) 16:Page 13 ofpeptidases), which can degrade other proteins (Fig. 7c), forming a double negative regulation cascade. The accumulation of such proteolytic enzymes in ask1 might cause decreased levels of their proteolytic substrates. Proteasome subunits and peptidases that accumulate in ask1 may perhaps be involved in degradati.THYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN-LIKE 2 (EGY2) UBIQUITIN-SPECIFIC PROTEASE five (UBP5) UBIQUITIN-SPECIFIC PROTEASE 6 (UBP6) 20S PROTEASOME ALPHA SUBUNIT E1 (PAE1) 20S PROTEASOME ALPHA SUBUNIT D2 (PAD2) 20S PROTEASOME BETA SUBUNIT C2 (PBC2) 20S PROTEASOME BETA SUBUNIT F1 (PBF1)AT2G40930 AT1G51710 AT1G53850 AT5G66140 AT1G77440 AT3Ginformation [https://dx.doi.org/10.1037/a0022827 title= a0022827] from expression and homology. Peptidases/ proteases might generally be topic to negative regulation by ASK1-E3s, therefore coupling peptidase-mediated protein processing or degradation with the UPS.Probable techniques that ASK1 regulates gene expressionFig. 7 Probable mechanisms of transcriptome and proteome regulations by ASK1-E3s. a ASK1-E3s may well regulate gene transcription by destabilizing transcription aspects. The transcription factors are stabilized in ask1 mutant and activate or repress downstream gene transcription. TF+, transcriptional activators; TF-, transcriptional repressors. b ASK1-E3s may well destabilize substrate X, which positively regulates the abundance of target proteins Y. In the ask1 mutant proteome, ASK1-E3 substrate X and their target protein Y accumulate. c ASK1-E3s might destabilize substrate X, which negatively regulates the abundance of target protein Y. Within the ask1 mutant proteome, ASK1-E3 substrate X accumulates but target protein Y decreases. Bars, negative regulation; horizontal arrows, good regulation; dashed gray bars and horizontal arrows, missing regulations; upward arrows, improve in abundance; downward arrows, reduce in abundanceBy integrative evaluation of transcriptome and proteome information, we discovered that ASK1-E3s could possibly regulate gene expression at many measures, ranging from transcriptional, translational, to post-translational regulations. ASK1-E3s may perhaps destabilize transcription repressors or activators to derepress or inactivate gene transcription, respectively (Fig. 7a). In the absence of ASK1, the accumulation of these transcriptional repressors or activators benefits in down-regulation or upregulation of gene transcription, respectively. On the other hand, we can not rule out the possibility that the altered transcriptome and proteome may be indirect consequences from the ask1 mutation. The proteins accumulated in ask1 could be direct substrates of ASK1-E3s, or stabilized by ASK1-E3 [https://dx.doi.org/10.1089/jir.2013.0113 title= jir.2013.0113] substrates (Fig. 7b). One example is, ubiquitin-specific proteases UBP5 and UBP6, which accumulate within the ask1 proteome (Table 7), could be substrates of ASK1-E3s; UBP5 and UBP6 could deubiquitinate and protect against degradation of ubiquitinated proteins, whose protein levels are then increased in ask1. An instance in human may be the herpesvirusassociated ubiquitin-specific protease (HAUSP), whichstabilizes a tumor suppressor p53 by deubiquitination [81]. Ribosomal proteins may possibly share a equivalent mechanism: accumulation of ribosomal proteins in ask1 may possibly enhance protein synthesis; alternatively, if ribosomal proteins have extraribosomal regulatory functions, they may stabilize some proteins in a comparable way as those stabilizing p53 in human [67]. | |
Версія за 13:13, 23 січня 2018
Within the Ess, 2010); I. McLean, The Legend of Red Clydeside (Edinburgh, Scotland: John absence of ASK1, the accumulation of those transcriptional repressors or activators benefits in down-regulation or upregulation of gene transcription, respectively. Ribosomal proteins could share a similar mechanism: accumulation of ribosomal proteins in ask1 might improve protein synthesis; alternatively, if ribosomal proteins have extraribosomal regulatory functions, they may stabilize some proteins in a related way as these stabilizing p53 in human [67]. In a further attainable situation, ASK1-E3s may well destabilize some proteolytic enzymes (e.g., E3 ubiquitin ligases orLu et al. BMC Plant Biology (2016) 16:Page 13 ofpeptidases), which can degrade other proteins (Fig. 7c), forming a double negative regulation cascade. The accumulation of such proteolytic enzymes in ask1 might cause decreased levels of their proteolytic substrates. Proteasome subunits and peptidases that accumulate in ask1 may perhaps be involved in degradati.THYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN-LIKE 2 (EGY2) UBIQUITIN-SPECIFIC PROTEASE five (UBP5) UBIQUITIN-SPECIFIC PROTEASE 6 (UBP6) 20S PROTEASOME ALPHA SUBUNIT E1 (PAE1) 20S PROTEASOME ALPHA SUBUNIT D2 (PAD2) 20S PROTEASOME BETA SUBUNIT C2 (PBC2) 20S PROTEASOME BETA SUBUNIT F1 (PBF1)AT2G40930 AT1G51710 AT1G53850 AT5G66140 AT1G77440 AT3Ginformation title= a0022827 from expression and homology. Peptidases/ proteases might generally be topic to negative regulation by ASK1-E3s, therefore coupling peptidase-mediated protein processing or degradation with the UPS.Probable techniques that ASK1 regulates gene expressionFig. 7 Probable mechanisms of transcriptome and proteome regulations by ASK1-E3s. a ASK1-E3s may well regulate gene transcription by destabilizing transcription aspects. The transcription factors are stabilized in ask1 mutant and activate or repress downstream gene transcription. TF+, transcriptional activators; TF-, transcriptional repressors. b ASK1-E3s may well destabilize substrate X, which positively regulates the abundance of target proteins Y. In the ask1 mutant proteome, ASK1-E3 substrate X and their target protein Y accumulate. c ASK1-E3s might destabilize substrate X, which negatively regulates the abundance of target protein Y. Within the ask1 mutant proteome, ASK1-E3 substrate X accumulates but target protein Y decreases. Bars, negative regulation; horizontal arrows, good regulation; dashed gray bars and horizontal arrows, missing regulations; upward arrows, improve in abundance; downward arrows, reduce in abundanceBy integrative evaluation of transcriptome and proteome information, we discovered that ASK1-E3s could possibly regulate gene expression at many measures, ranging from transcriptional, translational, to post-translational regulations. ASK1-E3s may perhaps destabilize transcription repressors or activators to derepress or inactivate gene transcription, respectively (Fig. 7a). In the absence of ASK1, the accumulation of these transcriptional repressors or activators benefits in down-regulation or upregulation of gene transcription, respectively. On the other hand, we can not rule out the possibility that the altered transcriptome and proteome may be indirect consequences from the ask1 mutation. The proteins accumulated in ask1 could be direct substrates of ASK1-E3s, or stabilized by ASK1-E3 title= jir.2013.0113 substrates (Fig. 7b). One example is, ubiquitin-specific proteases UBP5 and UBP6, which accumulate within the ask1 proteome (Table 7), could be substrates of ASK1-E3s; UBP5 and UBP6 could deubiquitinate and protect against degradation of ubiquitinated proteins, whose protein levels are then increased in ask1. An instance in human may be the herpesvirusassociated ubiquitin-specific protease (HAUSP), whichstabilizes a tumor suppressor p53 by deubiquitination [81]. Ribosomal proteins may possibly share a equivalent mechanism: accumulation of ribosomal proteins in ask1 may possibly enhance protein synthesis; alternatively, if ribosomal proteins have extraribosomal regulatory functions, they may stabilize some proteins in a comparable way as those stabilizing p53 in human [67].
