scholarly journals Temporal Proteomics of Inducible RNAi Lines of Clp Protease Subunits Identifies Putative Protease Substrates

2017 ◽  
Vol 176 (2) ◽  
pp. 1485-1508 ◽  
Author(s):  
Juan C. Moreno ◽  
Silvia Martínez-Jaime ◽  
Joram Schwartzmann ◽  
Daniel Karcher ◽  
Michael Tillich ◽  
...  
Keyword(s):  
Clp Protease ◽  
Putative Protease ◽  
Inducible Rnai

scholarly journals Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli.

1993 ◽  
Vol 268 (30) ◽  
pp. 22609-22617 ◽  
Author(s):  
D Wojtkowiak ◽  
C Georgopoulos ◽  
M Zylicz
Keyword(s):  
Escherichia Coli ◽  
Clp Protease ◽  
Isolation And Characterization

Proteomic Analysis of the Acid-Soluble Nacre Matrix of the Bivalve Unio pictorum: Detection of Novel Carbonic Anhydrase and Putative Protease Inhibitor Proteins

ChemBioChem ◽  
2010 ◽  
Vol 11 (15) ◽  
pp. 2138-2147 ◽  
Author(s):  
Benjamin Marie ◽  
Isabelle Zanella-Cléon ◽  
Nathalie Le Roy ◽  
Michel Becchi ◽  
Gilles Luquet ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Protease Inhibitor ◽  
Proteomic Analysis ◽  
Putative Protease ◽  
Unio Pictorum

scholarly journals Post-Translational Regulation via Clp Protease Is Critical for Survival of Mycobacterium tuberculosis

2014 ◽  
Vol 10 (3) ◽  
pp. e1003994 ◽  
Author(s):  
Ravikiran M. Raju ◽  
Mark P. Jedrychowski ◽  
Jun-Rong Wei ◽  
Jessica T. Pinkham ◽  
Annie S. Park ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Translational Regulation ◽  
Clp Protease

scholarly journals ClpS1 Is a Conserved Substrate Selector for the Chloroplast Clp Protease System in Arabidopsis

2013 ◽  
Vol 25 (6) ◽  
pp. 2276-2301 ◽  
Author(s):  
K. Nishimura ◽  
Y. Asakura ◽  
G. Friso ◽  
J. Kim ◽  
S.-h. Oh ◽  
...  
Keyword(s):  
Clp Protease

scholarly journals Initial Characterization of the Two ClpP Paralogs ofChlamydia trachomatisSuggests Unique Functionality for Each

2018 ◽  
Vol 201 (2) ◽  
Author(s):  
Nicholas A. Wood ◽  
Krystal Y. Chung ◽  
Amanda M. Blocker ◽  
Nathalia Rodrigues de Almeida ◽  
Martin Conda-Sheridan ◽  
...  
Keyword(s):  
Host Cells ◽  
Developmental Cycle ◽  
Intracellular Bacteria ◽  
Clp Protease ◽  
Content Type ◽  
Sexually Transmitted ◽  
Obligate Intracellular ◽  
Developmental Form ◽  
Obligate Intracellular Bacteria

ABSTRACTMembers ofChlamydiaare obligate intracellular bacteria that differentiate between two distinct functional and morphological forms during their developmental cycle, elementary bodies (EBs) and reticulate bodies (RBs). EBs are nondividing small electron-dense forms that infect host cells. RBs are larger noninfectious replicative forms that develop within a membrane-bound vesicle, termed an inclusion. Given the unique properties of each developmental form of this bacterium, we hypothesized that the Clp protease system plays an integral role in proteomic turnover by degrading specific proteins from one developmental form or the other.Chlamydiaspp. have five uncharacterizedclpgenes,clpX,clpC, twoclpPparalogs, andclpB. In other bacteria, ClpC and ClpX are ATPases that unfold and feed proteins into the ClpP protease to be degraded, and ClpB is a deaggregase. Here, we focused on characterizing the ClpP paralogs. Transcriptional analyses and immunoblotting determined that these genes are expressed midcycle. Bioinformatic analyses of these proteins identified key residues important for activity. Overexpression of inactiveclpPmutants inChlamydiaspp. suggested independent function of each ClpP paralog. To further probe these differences, we determined interactions between the ClpP proteins using bacterial two-hybrid assays and native gel analysis of recombinant proteins. Homotypic interactions of the ClpP proteins, but not heterotypic interactions between the ClpP paralogs, were detected. Interestingly, protease activity of ClpP2, but not ClpP1, was detectedin vitro. This activity was stimulated by antibiotics known to activate ClpP, which also blocked chlamydial growth. Our data suggest the chlamydial ClpP paralogs likely serve distinct and critical roles in this important pathogen.IMPORTANCEChlamydia trachomatisis the leading cause of preventable infectious blindness and of bacterial sexually transmitted infections worldwide. Chlamydiae are developmentally regulated obligate intracellular pathogens that alternate between two functional and morphologic forms, with distinct repertoires of proteins. We hypothesize that protein degradation is a critical aspect to the developmental cycle. A key system involved in protein turnover in bacteria is the Clp protease system. Here, we characterized the two chlamydial ClpP paralogs by examining their expression inChlamydiaspp., their ability to oligomerize, and their proteolytic activity. This work will help understand the evolutionarily diverse Clp proteases in the context of intracellular organisms, which may aid in the study of other clinically relevant intracellular bacteria.

scholarly journals PfClpC Is an Essential Clp Chaperone Required for Plastid Integrity and Clp Protease Stability in Plasmodium falciparum

Cell Reports ◽  
2017 ◽  
Vol 21 (7) ◽  
pp. 1746-1756 ◽  
Author(s):  
Anat Florentin ◽  
David W. Cobb ◽  
Jillian D. Fishburn ◽  
Michael J. Cipriano ◽  
Paul S. Kim ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Clp Protease ◽  
Protease Stability

Interaction specificity between the chaperone and proteolytic components of the cyanobacterial Clp protease

2012 ◽  
Vol 446 (2) ◽  
pp. 311-320 ◽  
Author(s):  
Anders Tryggvesson ◽  
Frida M. Ståhlberg ◽  
Axel Mogk ◽  
Kornelius Zeth ◽  
Adrian K. Clarke
Keyword(s):  
Escherichia Coli ◽  
Active Sites ◽  
Terminal Sequence ◽  
Core Complex ◽  
Clp Protease ◽  
E Coli ◽  
Loop Region ◽  
N Terminus ◽  
Specific Association ◽  
The Stability

The Clp protease is conserved among eubacteria and most eukaryotes, and uses ATP to drive protein substrate unfolding and translocation into a chamber of sequestered proteolytic active sites. In plant chloroplasts and cyanobacteria, the essential constitutive Clp protease consists of the Hsp100/ClpC chaperone partnering a proteolytic core of catalytic ClpP and noncatalytic ClpR subunits. In the present study, we have examined putative determinants conferring the highly specific association between ClpC and the ClpP3/R core from the model cyanobacterium Synechococcus elongatus. Two conserved sequences in the N-terminus of ClpR (tyrosine and proline motifs) and one in the N-terminus of ClpP3 (MPIG motif) were identified as being crucial for the ClpC–ClpP3/R association. These N-terminal domains also influence the stability of the ClpP3/R core complex itself. A unique C-terminal sequence was also found in plant and cyanobacterial ClpC orthologues just downstream of the P-loop region previously shown in Escherichia coli to be important for Hsp100 association to ClpP. This R motif in Synechococcus ClpC confers specificity for the ClpP3/R core and prevents association with E. coli ClpP; its removal from ClpC reverses this core specificity.

scholarly journals A chemical-regulated inducible RNAi system in plants

2003 ◽  
Vol 34 (3) ◽  
pp. 383-392 ◽  
Author(s):  
Hui-Shan Guo ◽  
Ji-Feng Fei ◽  
Qi Xie ◽  
Nam-Hai Chua
Keyword(s):  
Inducible Rnai

Effects of light and temperature on expression of ClpC, the regulatory subunit of chloroplastic Clp protease, in pea seedlings

1996 ◽  
Vol 31 (3) ◽  
pp. 673-676 ◽  
Author(s):  
Oren Ostersetzer ◽  
Zach Adam
Keyword(s):  
Regulatory Subunit ◽  
Clp Protease ◽  
Pea Seedlings
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