Results 11 to 20 of about 171,782 (185)

Contribution of the Clp Protease to Bacterial Survival and Mitochondrial Homoeostasis [PDF]

Microbial Physiology, 2021
Fast adaptation to environmental changes ensures bacterial survival, and proteolysis represents a key cellular process in adaptation. The Clp protease system is a multi-component machinery responsible for protein homoeostasis, protein quality control, and targeted proteolysis of transcriptional regulators in prokaryotic cells and prokaryote-derived ...
Astrid, Illigmann, Yvonne, Thoma, Stefan, Pan, Laura, Reinhardt, Heike, Brötz-Oesterhelt   +4 more
openaire   +3 more sources

Conformational control of the bacterial Clp protease by natural product antibiotics

Natural Product Reports, 2017
Natural products targeting the bacterial Clp protease unravel key interfaces for protein–protein–interaction and long-distance conformational control.
I. T. Malik, H. Brötz-Oesterhelt
openaire   +4 more sources

Control of plastidial metabolism by the Clp protease complex [PDF]

Journal of Experimental Botany, 2018
Plant metabolism is strongly dependent on plastids. Besides hosting the photosynthetic machinery, these endosymbiotic organelles synthesize starch, fatty acids, amino acids, nucleotides, tetrapyrroles, and isoprenoids. Virtually all enzymes involved in plastid-localized metabolic pathways are encoded by the nuclear genome and imported into plastids ...
Manuel Rodriguez-Concepcion, Lucio D’Andrea, Pablo Pulido   +2 more
openaire   +6 more sources

Structure and Function of a Novel Type of ATP-dependent Clp Protease [PDF]

Journal of Biological Chemistry, 2009
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. The main constitutive Clp protease in photosynthetic organisms has evolved into a functionally essential and structurally intricate enzyme. The model Clp protease
Andersson, F., Tryggvesson, A., Sharon, M., Diemand, A., Classen, M., Best, C., Schmidt, R., Schelin, J., Stanne, T., Bukau, B., Robinson, C., Witt, S., Mogk, A., Clarke, A.   +13 more
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Distinctive Types of ATP-dependent Clp Proteases in Cyanobacteria [PDF]

Journal of Biological Chemistry, 2007
Cyanobacteria are the only prokaryotes that perform oxygenic photosynthesis and are thought to be ancestors to plant chloroplasts. Like chloroplasts, cyanobacteria possess a diverse array of proteolytic enzymes, with one of the most prominent being the ATP-dependent Ser-type Clp protease.
Tara M, Stanne, Elena, Pojidaeva, Fredrik I, Andersson, Adrian K, Clarke   +3 more
openaire   +3 more sources

Actinobacterial Clp protease evolutionary diversity and substrate recognition

, 2022
The Actinomycetota (synonym Actinobacteria) are one of the largest bacterial phyla and are widely distributed in nature, playing roles in nutrient cycling, as microbiome members, and as human pathogens. The actinobacterial species Mycobacterium tuberculosis (Mtb) causes tuberculosis (TB), which is one of the leading causes of infectious mortality ...
Jiang, Jialiu
openaire   +3 more sources

The ATP‐dependent Clp protease in chloroplasts of higher plants

Physiologia Plantarum, 2005
The best‐known proteases in plastids are those that belong to families common to eubacteria. One of the first identified was the ATP‐dependent caseinolytic protease (Clp), whose structure and function have been well characterized in Escherichia coli. Plastid Clp proteins in higher plants are surprisingly numerous and diverse, with at least 16 distinct
Adrian K. Clarke, Tara M. MacDonald, Lars L. E. Sjögren   +2 more
openaire   +2 more sources

Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes.

Proceedings of the National Academy of Sciences, 1990
Bacteria, tomatoes, and trypanosomes all contain genes for a large protein with extensive homology to the regulatory subunit, ClpA, of the ATP-dependent protease of Escherichia coli, Clp. All members of the family have between 756 and 926 amino acids and contain two large regions, of 233 and 192 amino acids, each containing consensus sequences for ...
Gottesman, Susan, Squires, Craig, Pichersky, Eran, Carrington, Mark, Hobbs, Matthew, Mattick, John S., Dalrymple, Brian, Kuramitsu, Howard, Shiroza, Teruaki, Foster, Toshi, Clark, William P., Ross, Barbara, Squires, Catherine L., Maurizi, Michael R.   +13 more
openaire   +6 more sources

The essential M. tuberculosis Clp protease is functionally asymmetric in vivo. [PDF]

Sci Adv, 2022
The Clp protease system is a promising, noncanonical drug target against Mycobacterium tuberculosis (Mtb). Unlike in Escherichia coli , the Mtb Clp protease consists of two distinct proteolytic subunits, ClpP1 and ClpP2, which hydrolyze substrates delivered by the chaperones ClpX and ClpC1 ...
d'Andrea FB, Poulton NC, Poulton NC, Froom R, Tam K, Campbell EA, Rock JM.   +6 more
europepmc   +3 more sources

Characterization of a Clp protease gene regulator and the reaeration response in Mycobacterium tuberculosis. [PDF]

PLoS ONE, 2010
Mycobacterium tuberculosis (MTB) enters a non-replicating state when exposed to low oxygen tension, a condition the bacillus encounters in granulomas during infection.
Ashley M Sherrid, Tige R Rustad, Gerard A Cangelosi, David R Sherman   +3 more
doaj   +4 more sources