scholarly journals Catalytic Cycling of Human Mitochondrial Lon Protease

2022 ◽  
Author(s):  
Inayathulla Mohammed ◽  
Kai A. Schmitz ◽  
Niko Schenck ◽  
Dimitrios Balasopoulos ◽  
Annika Topitsch ◽  
...  
Keyword(s):  
Lon Protease

scholarly journals Synthesis, processing, and localization of human Lon protease.

1994 ◽  
Vol 269 (46) ◽  
pp. 29308-29313
Author(s):  
N Wang ◽  
M R Maurizi ◽  
L Emmert-Buck ◽  
M M Gottesman
Keyword(s):  
Lon Protease

Lon protease negatively affects GacA protein stability and expression of the Gac/Rsm signal transduction pathway inPseudomonas protegens

2014 ◽  
Vol 16 (8) ◽  
pp. 2538-2549 ◽  
Author(s):  
Kasumi Takeuchi ◽  
Wataru Tsuchiya ◽  
Naomi Noda ◽  
Rintaro Suzuki ◽  
Toshimasa Yamazaki ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Stability ◽  
Signal Transduction Pathway ◽  
Lon Protease ◽  
Transduction Pathway

scholarly journals Turnover of Mitochondrial Steroidogenic Acute Regulatory (StAR) Protein by Lon Protease: The Unexpected Effect of Proteasome Inhibitors

2007 ◽  
Vol 21 (9) ◽  
pp. 2164-2177 ◽  
Author(s):  
Zvi Granot ◽  
Oren Kobiler ◽  
Naomi Melamed-Book ◽  
Sarah Eimerl ◽  
Assaf Bahat ◽  
...  
Keyword(s):  
Proteasome Inhibitors ◽  
Lon Protease ◽  
Star Protein ◽  
Unexpected Effect ◽  
Steroidogenic Acute Regulatory

scholarly journals Mitochondrial Lon protease is a gatekeeper for proteins newly imported into the matrix

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Yuichi Matsushima ◽  
Kazuya Takahashi ◽  
Song Yue ◽  
Yuki Fujiyoshi ◽  
Hideaki Yoshioka ◽  
...  
Keyword(s):  
Protease Activity ◽  
Matrix Protein ◽  
Protein Import ◽  
Atp Hydrolysis ◽  
Lon Protease ◽  
Mitochondrial Matrix ◽  
The Matrix ◽  
Specific Proteins ◽  
Aggregation Activity ◽  
Hydrolysis Activity

AbstractHuman ATP-dependent Lon protease (LONP1) forms homohexameric, ring-shaped complexes. Depletion of LONP1 causes aggregation of a broad range of proteins in the mitochondrial matrix and decreases the levels of their soluble forms. The ATP hydrolysis activity, but not protease activity, of LONP1 is critical for its chaperone-like anti-aggregation activity. LONP1 forms a complex with the import machinery and an incoming protein, and protein aggregation is linked with matrix protein import. LONP1 also contributes to the degradation of imported, aberrant, unprocessed proteins using its protease activity. Taken together, our results show that LONP1 functions as a gatekeeper for specific proteins imported into the mitochondrial matrix.

scholarly journals Lon Protease Has Multifaceted Biological Functions inAcinetobacter baumannii

2018 ◽  
Vol 201 (2) ◽  
Author(s):  
Carly Ching ◽  
Brendan Yang ◽  
Chineme Onwubueke ◽  
David Lazinski ◽  
Andrew Camilli ◽  
...  
Keyword(s):  
Acinetobacter Baumannii ◽  
Biofilm Formation ◽  
Developmental Process ◽  
Cell Envelope ◽  
Opportunistic Pathogen ◽  
Lon Protease ◽  
Content Type ◽  
Hospital Acquired Infections ◽  
Biofilm Development ◽  
Hospital Acquired

ABSTRACTAcinetobacter baumanniiis a Gram-negative opportunistic pathogen that is known to survive harsh environmental conditions and is a leading cause of hospital-acquired infections. Specifically, multicellular communities (known as biofilms) ofA. baumanniican withstand desiccation and survive on hospital surfaces and equipment. Biofilms are bacteria embedded in a self-produced extracellular matrix composed of proteins, sugars, and/or DNA. Bacteria in a biofilm are protected from environmental stresses, including antibiotics, which provides the bacteria with selective advantage for survival. Although some gene products are known to play roles in this developmental process inA. baumannii, mechanisms and signaling remain mostly unknown. Here, we find that Lon protease inA. baumanniiaffects biofilm development and has other important physiological roles, including motility and the cell envelope. Lon proteases are found in all domains of life, participating in regulatory processes and maintaining cellular homeostasis. These data reveal the importance of Lon protease in influencing keyA. baumanniiprocesses to survive stress and to maintain viability.IMPORTANCEAcinetobacter baumanniiis an opportunistic pathogen and is a leading cause of hospital-acquired infections.A. baumanniiis difficult to eradicate and to manage, because this bacterium is known to robustly survive desiccation and to quickly gain antibiotic resistance. We sought to investigate biofilm formation inA. baumannii, since much remains unknown about biofilm formation in this bacterium. Biofilms, which are multicellular communities of bacteria, are surface attached and difficult to eliminate from hospital equipment and implanted devices. Our research identifies multifaceted physiological roles for the conserved bacterial protease Lon inA. baumannii. These roles include biofilm formation, motility, and viability. This work broadly affects and expands understanding of the biology ofA. baumannii, which will permit us to find effective ways to eliminate the bacterium.

scholarly journals Regulation of igaA and the Rcs System by the MviA Response Regulator in Salmonella enterica

2009 ◽  
Vol 191 (8) ◽  
pp. 2743-2752 ◽  
Author(s):  
Clara B. García-Calderón ◽  
Josep Casadesús ◽  
Francisco Ramos-Morales
Keyword(s):  
Membrane Protein ◽  
Salmonella Enterica ◽  
Response Regulator ◽  
Regulatory System ◽  
Enteric Bacteria ◽  
Lon Protease ◽  
Dependent Manner ◽  
Independent Manner ◽  
Serovar Typhimurium

ABSTRACT IgaA is a membrane protein that prevents overactivation of the Rcs regulatory system in enteric bacteria. Here we provide evidence that igaA is the first gene in a σ70-dependent operon of Salmonella enterica serovar Typhimurium that also includes yrfG, yrfH, and yrfI. We also show that the Lon protease and the MviA response regulator participate in regulation of the igaA operon. Our results indicate that MviA regulates igaA transcription in an RpoS-dependent manner, but the results also suggest that MviA may regulate RcsB activation in an RpoS- and IgaA-independent manner.

Sign in / Sign up

Export Citation Format

Share Document