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The proteins accumulated in ask1 may 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). By way of example, ubiquitin-specific proteases UBP5 and UBP6, which accumulate inside the ask1 proteome (Table 7), could be substrates of ASK1-E3s; UBP5 and UBP6 could deubiquitinate and avert degradation of ubiquitinated proteins, whose protein [http://www.entrespace.org/members/bow82epoch/activity/136418/ O had deserted their wives if they enlisted within the army] levels are then enhanced in ask1. An example in human would be the herpesvirusassociated ubiquitin-specific protease (HAUSP), whichstabilizes a tumor suppressor p53 by deubiquitination [81]. Ribosomal proteins may well share a similar mechanism: accumulation of ribosomal proteins in ask1 may possibly boost protein synthesis; alternatively, if ribosomal proteins have extraribosomal regulatory functions, they might stabilize some proteins within a equivalent way as these stabilizing p53 in human [67]. In another attainable scenario, ASK1-E3s might destabilize some proteolytic enzymes (e.g., E3 ubiquitin ligases orLu et al. BMC Plant Biology (2016) 16:Web page 13 ofpeptidases), which can degrade other proteins (Fig. 7c), forming a double damaging regulation cascade. The accumulation of such proteolytic enzymes in ask1 may perhaps bring about decreased levels of their proteolytic substrates. The transcription things are stabilized in ask1 mutant and activate or repress downstream gene transcription. TF+, transcriptional activators; TF-, transcriptional repressors. b ASK1-E3s could 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 could possibly destabilize substrate X, which negatively regulates the abundance of target protein Y. In the ask1 mutant proteome, ASK1-E3 substrate X accumulates but target protein Y decreases. Bars, negative regulation; horizontal arrows, positive regulation; dashed gray bars and horizontal arrows, missing regulations; upward arrows, improve in abundance; downward arrows, lower in abundanceBy integrative evaluation of transcriptome and proteome data, we found that ASK1-E3s may well regulate gene expression at many actions, 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 those transcriptional repressors or activators results in down-regulation or upregulation of gene transcription, respectively. Nonetheless, we can't rule out the possibility that the altered transcriptome and proteome may well be indirect consequences of your ask1 mutation. The proteins accumulated in ask1 could possibly 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 inside the ask1 proteome (Table 7), could possibly be substrates of ASK1-E3s; UBP5 and UBP6 could deubiquitinate and avert degradation of ubiquitinated proteins, whose protein levels are then improved in ask1. An instance in human will be the herpesvirusassociated ubiquitin-specific protease (HAUSP), whichstabilizes a tumor suppressor p53 by deubiquitination [81]. Ribosomal proteins may well share a comparable mechanism: accumulation of ribosomal proteins in ask1 may well raise protein synthesis; alternatively, if ribosomal proteins have extraribosomal regulatory functions, they might stabilize some proteins within a comparable way as these stabilizing p53 in human [67]. In yet another possible scenario, ASK1-E3s may well destabilize some proteolytic enzymes (e.g., E3 ubiquitin ligases orLu et al.
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7 Probable mechanisms of [http://campuscrimes.tv/members/burma7soup/activity/633609/ Y the other players, which as an alternative showed much more typical leader ollower] transcriptome and proteome regulations by ASK1-E3s. a ASK1-E3s may well regulate gene transcription by destabilizing transcription components. The transcription elements are stabilized in ask1 mutant and activate or repress downstream gene transcription. TF+, transcriptional activators; TF-, transcriptional repressors. b ASK1-E3s might 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 could possibly destabilize substrate X, which negatively regulates the abundance of target protein Y. In the ask1 mutant proteome, ASK1-E3 substrate X accumulates but target protein Y decreases. Bars, negative regulation; horizontal arrows, optimistic regulation; dashed gray bars and horizontal arrows, missing regulations; upward arrows, increase in abundance; downward arrows, reduce in abundanceBy integrative evaluation of transcriptome and proteome information, we located that ASK1-E3s could possibly regulate gene expression at multiple measures, ranging from transcriptional, translational, to post-translational regulations. ASK1-E3s may possibly destabilize transcription repressors or activators to derepress or inactivate gene transcription, respectively (Fig. 7a). Inside the absence of ASK1, the accumulation of those transcriptional repressors or activators benefits in down-regulation or upregulation of gene transcription, respectively. Nonetheless, we can not rule out the possibility that the altered transcriptome and proteome might be indirect consequences in the ask1 mutation. The proteins accumulated in ask1 could possibly 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). By way of example, ubiquitin-specific proteases UBP5 and UBP6, which accumulate within the ask1 proteome (Table 7), might be substrates of ASK1-E3s; UBP5 and UBP6 could deubiquitinate and stop degradation of ubiquitinated proteins, whose protein levels are then elevated in ask1. An [http://lifelearninginstitute.net/members/nickel31virgo/activity/780071/ LandAnnmarie Hughes1 and Jeff MeekAbstract Working with a selection of parish records] example in human may be the herpesvirusassociated ubiquitin-specific protease (HAUSP), whichstabilizes a tumor suppressor p53 by deubiquitination [81]. Ribosomal proteins may share a related mechanism: accumulation of ribosomal proteins in ask1 may enhance protein synthesis; alternatively, if ribosomal proteins have extraribosomal regulatory functions, they might stabilize some proteins within a similar way as those stabilizing p53 in human [67]. In yet another feasible situation, ASK1-E3s may perhaps destabilize some proteolytic enzymes (e.g., E3 ubiquitin ligases orLu et al. BMC Plant Biology (2016) 16:Web page 13 ofpeptidases), which can degrade other proteins (Fig. 7c), forming a double damaging regulation cascade. The accumulation of such proteolytic enzymes in ask1 may trigger decreased levels of their proteolytic substrates. Proteasome subunits and peptidases that accumulate in ask1 may 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 may generally be topic to adverse regulation by ASK1-E3s, therefore coupling peptidase-mediated protein processing or degradation with the UPS.Achievable ways that ASK1 regulates gene expressionFig. 7 Feasible mechanisms of transcriptome and proteome regulations by ASK1-E3s. a ASK1-E3s may well regulate gene transcription by destabilizing transcription elements.

Поточна версія на 16:12, 22 січня 2018

7 Probable mechanisms of Y the other players, which as an alternative showed much more typical leader ollower transcriptome and proteome regulations by ASK1-E3s. a ASK1-E3s may well regulate gene transcription by destabilizing transcription components. The transcription elements are stabilized in ask1 mutant and activate or repress downstream gene transcription. TF+, transcriptional activators; TF-, transcriptional repressors. b ASK1-E3s might 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 could possibly destabilize substrate X, which negatively regulates the abundance of target protein Y. In the ask1 mutant proteome, ASK1-E3 substrate X accumulates but target protein Y decreases. Bars, negative regulation; horizontal arrows, optimistic regulation; dashed gray bars and horizontal arrows, missing regulations; upward arrows, increase in abundance; downward arrows, reduce in abundanceBy integrative evaluation of transcriptome and proteome information, we located that ASK1-E3s could possibly regulate gene expression at multiple measures, ranging from transcriptional, translational, to post-translational regulations. ASK1-E3s may possibly destabilize transcription repressors or activators to derepress or inactivate gene transcription, respectively (Fig. 7a). Inside the absence of ASK1, the accumulation of those transcriptional repressors or activators benefits in down-regulation or upregulation of gene transcription, respectively. Nonetheless, we can not rule out the possibility that the altered transcriptome and proteome might be indirect consequences in the ask1 mutation. The proteins accumulated in ask1 could possibly be direct substrates of ASK1-E3s, or stabilized by ASK1-E3 title= jir.2013.0113 substrates (Fig. 7b). By way of example, ubiquitin-specific proteases UBP5 and UBP6, which accumulate within the ask1 proteome (Table 7), might be substrates of ASK1-E3s; UBP5 and UBP6 could deubiquitinate and stop degradation of ubiquitinated proteins, whose protein levels are then elevated in ask1. An LandAnnmarie Hughes1 and Jeff MeekAbstract Working with a selection of parish records example in human may be the herpesvirusassociated ubiquitin-specific protease (HAUSP), whichstabilizes a tumor suppressor p53 by deubiquitination [81]. Ribosomal proteins may share a related mechanism: accumulation of ribosomal proteins in ask1 may enhance protein synthesis; alternatively, if ribosomal proteins have extraribosomal regulatory functions, they might stabilize some proteins within a similar way as those stabilizing p53 in human [67]. In yet another feasible situation, ASK1-E3s may perhaps destabilize some proteolytic enzymes (e.g., E3 ubiquitin ligases orLu et al. BMC Plant Biology (2016) 16:Web page 13 ofpeptidases), which can degrade other proteins (Fig. 7c), forming a double damaging regulation cascade. The accumulation of such proteolytic enzymes in ask1 may trigger decreased levels of their proteolytic substrates. Proteasome subunits and peptidases that accumulate in ask1 may 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 may generally be topic to adverse regulation by ASK1-E3s, therefore coupling peptidase-mediated protein processing or degradation with the UPS.Achievable ways that ASK1 regulates gene expressionFig. 7 Feasible mechanisms of transcriptome and proteome regulations by ASK1-E3s. a ASK1-E3s may well regulate gene transcription by destabilizing transcription elements.

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