Difference between revisions of "Part:BBa K3121000"
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At low temperatures, the usual rate-limiting step for efficient growth is protein folding. In fact, the regular chaperone systems, for instance, the GroEL/ES are also faced with significant challenges at colder conditions, which severely hamper their activity. This leads to a dramatic decrease in bacterial growth and proliferation. | At low temperatures, the usual rate-limiting step for efficient growth is protein folding. In fact, the regular chaperone systems, for instance, the GroEL/ES are also faced with significant challenges at colder conditions, which severely hamper their activity. This leads to a dramatic decrease in bacterial growth and proliferation. | ||
The TF, in essence, is a cold-active chaperone, which is significantly upregulated at low temperatures. This is especially helpful because unlike standard chaperones, the TF has a very unique operational mechanism - it requires near-zero temperatures to stably bind unfolded polypeptides. Under cold conditions, the TF will find almost all the newly synthesized polypeptides, and thereby rescue the chaperone function of the cold-inactivated GroEL/ES (and similar chaperone complexes like the DnaK). Additionally, the TF is a monomeric chaperone unit, which has considerable structural flexibility in order to compensate for the reduced molecular motions at lower temperatures. | The TF, in essence, is a cold-active chaperone, which is significantly upregulated at low temperatures. This is especially helpful because unlike standard chaperones, the TF has a very unique operational mechanism - it requires near-zero temperatures to stably bind unfolded polypeptides. Under cold conditions, the TF will find almost all the newly synthesized polypeptides, and thereby rescue the chaperone function of the cold-inactivated GroEL/ES (and similar chaperone complexes like the DnaK). Additionally, the TF is a monomeric chaperone unit, which has considerable structural flexibility in order to compensate for the reduced molecular motions at lower temperatures. | ||
| − | Interestingly enough, the TF is not an essential gene under mesophilic growth conditions - indicating a specialized adaptive role. Moreover, the niche (yet indispensable) requirement of TF is underscored by the fact that the other two major chaperone systems - GroEL/ES and DnaK are significantly downregulated, as well as inactivated, under cold conditions - thereby making the TF system the only chaperon in this scenario. | + | Interestingly enough, the TF is not an essential gene under mesophilic growth conditions - indicating a specialized adaptive role. Moreover, the niche (yet indispensable) requirement of TF is underscored by the fact that the other two major chaperone systems - GroEL/ES and DnaK are significantly downregulated, as well as inactivated, under cold conditions - thereby making the TF system the only chaperon in this scenario.hsajcsa |
Revision as of 18:26, 16 October 2019
Trigger Factor of P.haloplanktis
At low temperatures, the usual rate-limiting step for efficient growth is protein folding. In fact, the regular chaperone systems, for instance, the GroEL/ES are also faced with significant challenges at colder conditions, which severely hamper their activity. This leads to a dramatic decrease in bacterial growth and proliferation. The TF, in essence, is a cold-active chaperone, which is significantly upregulated at low temperatures. This is especially helpful because unlike standard chaperones, the TF has a very unique operational mechanism - it requires near-zero temperatures to stably bind unfolded polypeptides. Under cold conditions, the TF will find almost all the newly synthesized polypeptides, and thereby rescue the chaperone function of the cold-inactivated GroEL/ES (and similar chaperone complexes like the DnaK). Additionally, the TF is a monomeric chaperone unit, which has considerable structural flexibility in order to compensate for the reduced molecular motions at lower temperatures. Interestingly enough, the TF is not an essential gene under mesophilic growth conditions - indicating a specialized adaptive role. Moreover, the niche (yet indispensable) requirement of TF is underscored by the fact that the other two major chaperone systems - GroEL/ES and DnaK are significantly downregulated, as well as inactivated, under cold conditions - thereby making the TF system the only chaperon in this scenario.hsajcsa
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]