Molecular Playground/ClpP: Difference between revisions
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Here, in the [http://openwetware.org/wiki/Chien Chien lab] of the University of Massachusetts-Amherst, we study how [http://en.wikipedia.org/wiki/Proteolysis proteolysis] plays a large part in protein quality control. The maintenance and timely destruction of protein levels plays an important role during cell homeostasis and cell transitions/differentiation, yet much of what governs these processes has to be fully understood. | Here, in the [http://openwetware.org/wiki/Chien Chien lab] of the University of Massachusetts-Amherst, we study how [http://en.wikipedia.org/wiki/Proteolysis proteolysis] plays a large part in protein quality control. The maintenance and timely destruction of protein levels plays an important role during cell homeostasis and cell transitions/differentiation, yet much of what governs these processes has to be fully understood. | ||
<StructureSection load='1yg6' size='400' side='right' caption='E. coli ClpP protease' scene='60/609790/Clpp-2/2'> | <StructureSection load='1yg6' size='400' side='right' caption='E. coli ClpP protease' scene='60/609790/Clpp-2/2'> | ||
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''E. coli'' ClpAP/[[Molecular_Playground/Hexameric_ClpX|ClpX]]P complexes play a critical role in maintaining protein homeostasis under several levels of quality control. Improperly folded or aggregated proteins are potential ClpP substrates based on properties of the associated regulatory element recognition. Targeted removal of aberrant proteins resulting from and rescue of stalled ribosomes by the SsrA tagging system are directly recognized and degraded by ClpAP/ClpXP complexes [http://www.ncbi.nlm.nih.gov/pubmed/9573050]. In ''E. coli'' ClpP and ClpP homologues found in other bacteria require regulatory elements to recognize and import proteins for destruction. To gain access to the active sites is tightly controlled and therefore a potential antimicrobial target where loss of regulation (for example, through use of acyldepsipeptides or ADEPs) literally digests the bacteria from the inside out [http://link.springer.com/chapter/10.1007/978-94-007-6787-4_24]. ''E. coli'' ClpAP and ClpXP has been used as a structural model for the 26 proteasome to gain insight into its workings [http://www.ncbi.nlm.nih.gov/pubmed/7623377][http://www.ncbi.nlm.nih.gov/pubmed/14990998]. | ''E. coli'' ClpAP/[[Molecular_Playground/Hexameric_ClpX|ClpX]]P complexes play a critical role in maintaining protein homeostasis under several levels of quality control. Improperly folded or aggregated proteins are potential ClpP substrates based on properties of the associated regulatory element recognition. Targeted removal of aberrant proteins resulting from and rescue of stalled ribosomes by the SsrA tagging system are directly recognized and degraded by ClpAP/ClpXP complexes [http://www.ncbi.nlm.nih.gov/pubmed/9573050]. In ''E. coli'' ClpP and ClpP homologues found in other bacteria require regulatory elements to recognize and import proteins for destruction. To gain access to the active sites is tightly controlled and therefore a potential antimicrobial target where loss of regulation (for example, through use of acyldepsipeptides or ADEPs) literally digests the bacteria from the inside out [http://link.springer.com/chapter/10.1007/978-94-007-6787-4_24]. ''E. coli'' ClpAP and ClpXP has been used as a structural model for the 26 proteasome to gain insight into its workings [http://www.ncbi.nlm.nih.gov/pubmed/7623377][http://www.ncbi.nlm.nih.gov/pubmed/14990998]. | ||
</StructureSection> | |||
== References == | == References == | ||
<references/> | <references/> | ||