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PMID:23907089
| Citation |
Li, K, Jiang, T, Yu, B, Wang, L, Gao, C, Ma, C, Xu, P and Ma, Y (2013) Escherichia coli transcription termination factor NusA: heat-induced oligomerization and chaperone activity. Sci Rep 3:2347 |
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| Abstract |
Escherichia coli NusA, an essential component of the RNA polymerase elongation complex, is involved in transcriptional elongation, termination, anti-termination, cold shock and stress-induced mutagenesis. In this study, we demonstrated that NusA can self-assemble into oligomers under heat shock conditions and that this property is largely determined by the C-terminal domain. In parallel with the self-assembly process, NusA also acquires chaperone activity. Furthermore, NusA overexpression results in the enhanced heat shock resistance of host cells, which may be due to the chaperone activity of NusA. Our results suggest that E. coli NusA can act as a protector to prevent protein aggregation under heat stress conditions in vitro and in the NusA-overexpressing strain. We propose a new hypothesis that NusA could serve as a molecular chaperone in addition to its functions as a transcription factor. However, it remains to be further investigated whether NusA has the same function under normal physiological conditions. |
| Links |
PubMed PMC3731644 Online version:10.1038/srep02347 |
| Keywords |
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| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0051259: protein complex oligomerization |
ECO:0000314: direct assay evidence used in manual assertion |
P |
In Figure 1, it is shown that under heat shock conditions NusA can form stable high molecular weight(HMW)oligomers. |
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See also
References
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