Results 51 to 60 of about 3,616 (191)

ClpXP Degrades SsrA-Tagged Proteins inStreptococcus pneumoniae [PDF]

Journal of Bacteriology, 2009
ABSTRACTBacterial proteins that are abnormally truncated due to incomplete mRNA or the presence of rare codons are extended by an SsrA tag during ribosome rescue in atrans-translation process important for maintaining protein quality. InEscherichia coli, the SsrA-tagged proteins become the target of the Tsp, Lon, FtsH, ClpXP, and ClpAP proteases.
Sarita, Ahlawat, Donald A, Morrison
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Gain of Spontaneous clpX Mutations Boosting Motility via Adaption to Environments in Escherichia coli

Frontiers in Bioengineering and Biotechnology, 2021
Motility is finely regulated and is crucial to bacterial processes including colonization and biofilm formation. There is a trade-off between motility and growth in bacteria with molecular mechanisms not fully understood.
Bingyu Li, Bingyu Li, Bingyu Li, Chaofan Hou, Xian Ju, Yong Feng, Zhi-Qiang Ye, Yunzhu Xiao, Mingyao Gu, Chunxiang Fu, Chaoliang Wei, Conghui You   +11 more
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Stepwise Unfolding of a β Barrel Protein by the AAA+ ClpXP Protease [PDF]

Journal of Molecular Biology, 2011
In the AAA+ ClpXP protease, ClpX uses the energy of ATP binding and hydrolysis to unfold proteins before translocating them into ClpP for degradation. For proteins with C-terminal ssrA tags, ClpXP pulls on the tag to initiate unfolding and subsequent degradation.
Nager, Andrew Ross, Sauer, Robert T., Baker, Tania   +2 more
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Degradation of the E. coli antitoxin MqsA by the proteolytic complex ClpXP is regulated by zinc occupancy and oxidation [PDF]

, 2022
It is well established that the antitoxins of toxin-antitoxin (TA) systems are selectively degraded by bacterial proteases in response to stress. However, how distinct stressors result in the selective degradation of specific antitoxins remain unanswered.
Vos, M.R., Wolfgang Peti, Rebecca Page, Rahmani, N., Trebino, C.E., Camberg, J.L., Benjamin Piraino, Vos, Margaret R., Rahmani, Negar, Catherine E. Trebino, Christopher J. LaBreck, Negar Rahmani, Trebino, Catherine E., LaBreck, Christopher J., Margaret R. Vos, Marta Schoenle, Piraino, Benjamin, LaBreck, C.J., Peti, Wolfgang, Camberg, Jodi L., Schoenle, M., Jodi L. Camberg, Piraino, B., Peti, W., Page, Rebecca, Schoenle, Marta, Page, R.   +26 more
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Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP [PDF]

Proceedings of the National Academy of Sciences, 2000
ClpX and ClpA are molecular chaperones that interact with specific proteins and, together with ClpP, activate their ATP-dependent degradation. The chaperone activity is thought to convert proteins into an extended conformation that can access the sequestered active sites of ClpP.
Singh, S.K., Grimaud, R., Hoskins, J.R., Wickner, S., Maurizi, M.R.   +4 more
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The Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpP

Frontiers in Molecular Biosciences, 2017
ClpX is a member of the Clp/Hsp100 family of ATP-dependent chaperones and partners with ClpP, a compartmentalized protease, to degrade protein substrates bearing specific recognition signals.
Christopher J. LaBreck, Shannon May, Marissa G. Viola, Joseph Conti, Jodi L. Camberg   +4 more
doaj   +1 more source

A Uniform Benchmark for Testing SsrA-Derived Degrons in the Escherichia coli ClpXP Degradation Pathway

Molecules, 2021
The ssrA degron is commonly used in fusion proteins to control protein stability in bacteria or as an interaction module. These applications often rely on the modular activities of the ssrA tag in binding to the SspB adaptor and in engaging the ClpXP ...
Maria Magdalena Klimecka, Anna Antosiewicz, Matylda Anna Izert, Patrycja Emanuela Szybowska, Piotr Krzysztof Twardowski, Clara Delaunay, Maria Wiktoria Górna   +6 more
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ClpXP controls the expression of LEE genes in enterohaemorrhagic Escherichia coli [PDF]

FEMS Microbiology Letters, 2005
Enterohaemorrhagic Escherichia coli (EHEC) contains a 36-kb pathogenicity island termed the locus of enterocyte effacement (LEE), which encodes a type III secretion system (TTSS) and virulence proteins. In this paper, we show that the O157:H7 Sakai clpPX mutant strongly impaired the secretion of virulence proteins by TTSS and repressed transcription ...
Toshifumi, Tomoyasu, Akiko, Takaya, Yutaka, Handa, Kiyonobu, Karata, Tomoko, Yamamoto   +4 more
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A split protease-E. coli ClpXP system quantifies protein–protein interactions in Escherichia coli cells

Communications Biology, 2021
Wang et al. developed a fluorescence-assisted single-cell methodology (split protease-E. coli ClpXP (SPEC)) to characterise protein-protein interactions for both eukaryotic and prokaryotic species in E. coli cells.
Shengchen Wang, Faying Zhang, Meng Mei, Ting Wang, Yueli Yun, Shihui Yang, Guimin Zhang, Li Yi   +7 more
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Serine and Threonine Phosphorylation Marks Proteins for Degradation By Clpxp

Blood, 2021
Abstract The mitochondrial serine protease, ClpXP, regulates the integrity of the respiratory chain by degrading damaged and/or misfolded proteins. This protease is over-expressed in a subset of AML and inhibiting or hyperactivating it kills leukemic cells and stem cells in vitro and in vivo.
Yue Feng, Yulia Jitkova, Harjeet Soor, Suzanne Trudel, Kaitlin Lees, Kaylen Soriano, Siavash Vahidi, Andrei Yudin, Aaron D Schimmer   +8 more
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