Production of Recombinant Rhomboid Proteases

2017 ◽  
pp. 255-278
Author(s):  
E. Arutyunova ◽  
R. Panigrahi ◽  
K. Strisovsky ◽  
M.J. Lemieux
Keyword(s):  
Rhomboid Proteases

scholarly journals Inhibitors of rhomboid proteases

Biochimie ◽  
2016 ◽  
Vol 122 ◽  
pp. 38-47 ◽  
Author(s):  
Eliane V. Wolf ◽  
Steven H.L. Verhelst
Keyword(s):  
Rhomboid Proteases

scholarly journals Rhomboid Proteases: Familiar Features in Unfamiliar Phases

2009 ◽  
Vol 36 (6) ◽  
pp. 922-923 ◽  
Author(s):  
Bilal Amarneh ◽  
Robert B. Rawson
Keyword(s):  
Rhomboid Proteases

scholarly journals General and Modular Strategy for Designing Potent, Selective, and Pharmacologically Compliant Inhibitors of Rhomboid Proteases

2017 ◽  
Vol 24 (12) ◽  
pp. 1523-1536.e4 ◽  
Author(s):  
Anežka Tichá ◽  
Stancho Stanchev ◽  
Kutti R. Vinothkumar ◽  
David C. Mikles ◽  
Petr Pachl ◽  
...  
Keyword(s):  
Rhomboid Proteases

scholarly journals New insights into parasite rhomboid proteases

2012 ◽  
Vol 182 (1-2) ◽  
pp. 27-36 ◽  
Author(s):  
Joana M. Santos ◽  
Arnault Graindorge ◽  
Dominique Soldati-Favre
Keyword(s):  
Rhomboid Proteases

scholarly journals Mitochondrial regulation in Dictyostelium discoideum

2018 ◽  
Author(s):  
Mehak Rafiq
Keyword(s):  
Dictyostelium Discoideum ◽  
Serine Proteases ◽  
Model Organism ◽  
Complex Life Cycle ◽  
Transcriptional Networks ◽  
Multicellular Development ◽  
Mitochondrial Regulation ◽  
Rhomboid Proteases ◽  
The Social ◽  
Membrane Bound

Proteolysis is increasingly documented as a method of regulation of mitochondrial function. Our studies of rhomboidfamily proteins’ roles in organelles show that this is also the case in the social amoeba Dictyostelium discoideum, in which four of these membrane-bound, evolutionarily ubiquitous, serine proteases are found. Rhomboid proteases act on disparate substrates in different organisms so far studied, but their mode of action is conserved: their location in the membrane means that their membrane-tethered substrates can act in signalling upon release, or be activated, by rhomboid-mediated cleavage. Among eukaryotic rhomboids is the mitochondrial protease ‘PARL’, which ensures the maintenance of the structural and functional integrity of mitochondria and plastids, but we have found that other Dictyostelium rhomboids also affect the organelle. Studying the development and behaviour of Dictyostelium, a microbial model organism with a complex life cycle that includes uni- and multicellular stages, allowed investigation of the role of rhomboids in unicellular vegetative growth, multicellular development and sporulation, phagocytosis, and response to the environment. We found that two rhomboid-null mutants gave rise to changes in development, rhmA altering the response to chemoattractants and demonstrating decreased motility in general, whereas rhmB null cells had slower growth rates with decreased response to folic acid. RhmA, although located in the contractile vacuole, affects the ultrastructure of mitochondria, and RhmB-GFP fusions protein was localised to the mitochondrion. qPCR analysis revealed RhmA and RhmB transcript levels peaking during the multicellular growth phase and transcriptional networks suggest the Dictyostelium rhmA is regulated along with the orthologues of Saccharomyces cerevisiae mitochondrial rhomboid substrates.

scholarly journals New insight into plant intramembrane proteases

2017 ◽  
Author(s):  
Małgorzata Adamiec ◽  
Lucyna Misztal ◽  
Robert Luciński
Keyword(s):  
Protein Turnover ◽  
Higher Plants ◽  
Protein Sequences ◽  
Higher Plant ◽  
Aspartic Proteases ◽  
Phylogenetic Relations ◽  
Intramembrane Proteases ◽  
Rhomboid Proteases ◽  
Zinc Metalloproteases ◽  
Insight Into

ABSTRACTThe process of proteolysis is a factor involved in control of the proper development of the plant and its responses to a changeable environment. Recent research has shown that proteases are not only engaged in quality control and protein turnover processes but also participate in the process which is known as regulated membrane proteolysis (RIP). Four families of integral membrane proteases, belonging to three different classes, have been identified: serine intramembrane proteases known as rhomboid proteases, site-2 proteases belonging to zinc metalloproteases, and two families of aspartic proteases: presenilins and signal peptide peptidases. The studies concerning intramembrane proteases in higher plants are, however, focused on Arabidopsis thaliana. The aim of the study was to identify and retrieve protein sequences of intramembrane protease homologs from other higher plant species and perform a detailed analysis of their primary sequences as well as their phylogenetic relations. This approach allows us to indicate several previously undescribed issues which may provide important directions for further research.

Biology of rhomboid proteases in infectious diseases

2016 ◽  
Vol 60 ◽  
pp. 38-45 ◽  
Author(s):  
Sunil Kumar Dogga ◽  
Dominique Soldati-Favre
Keyword(s):  
Infectious Diseases ◽  
Rhomboid Proteases

scholarly journals Substrates and physiological functions of secretase rhomboid proteases

2016 ◽  
Vol 60 ◽  
pp. 10-18 ◽  
Author(s):  
Viorica L. Lastun ◽  
Adam G. Grieve ◽  
Matthew Freeman
Keyword(s):  
Physiological Functions ◽  
Rhomboid Proteases
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