Results 11 to 20 of about 17,783 (200)

Arginine phosphorylation marks proteins for degradation by a Clp protease. [PDF]

open access: yesNature, 2016
Protein turnover is a tightly controlled process that is crucial for the removal of aberrant polypeptides and for cellular signalling. Whereas ubiquitin marks eukaryotic proteins for proteasomal degradation, a general tagging system for the equivalent bacterial Clp proteases is not known.
Trentini DB   +6 more
europepmc   +6 more sources

The Clp protease system; a central component of the chloroplast protease network

open access: yesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2011
Intra-plastid proteases play crucial and diverse roles in the development and maintenance of non-photosynthetic plastids and chloroplasts. Formation and maintenance of a functional thylakoid electron transport chain requires various protease activities, operating in parallel, as well as in series. This review first provides a short, referenced overview
Olinares, Paul Dominic B.   +2 more
openaire   +4 more sources

Conformational control of the bacterial Clp protease by natural product antibiotics

open access: yesNatural 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   +5 more sources

Organization, function and substrates of the essential Clp protease system in plastids

open access: yesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2015
Intra-plastid proteolysis is essential in plastid biogenesis, differentiation and plastid protein homeostasis (proteostasis). We provide a comprehensive review of the Clp protease system present in all plastid types and we draw lessons from structural and functional information of bacterial Clp systems.
Nishimura, Kenji, van Wijk, Klaas J.
openaire   +4 more sources

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

open access: yesSci 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   +5 more
europepmc   +3 more sources

Interference with Clp protease impairs carotenoid accumulation during tomato fruit ripening. [PDF]

open access: yesJ Exp Bot, 2018
Profound metabolic and structural changes are required for fleshy green fruits to ripen and become colorful and tasty. In tomato (Solanum lycopersicum), fruit ripening involves the differentiation of chromoplasts, specialized plastids that accumulate carotenoid pigments such as β-carotene (pro-vitamin A) and lycopene.
D'Andrea L   +7 more
europepmc   +7 more sources

Antibiotic Acyldepsipeptides Stimulate the Streptomyces Clp-ATPase/ClpP Complex for Accelerated Proteolysis

open access: yesmBio, 2022
Clp proteases consist of a proteolytic, tetradecameric ClpP core and AAA+ Clp-ATPases. Streptomycetes, producers of a plethora of secondary metabolites, encode up to five different ClpP homologs, and the composition of their unusually complex Clp ...
Laura Reinhardt   +7 more
doaj   +1 more source

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

open access: yesMicrobial 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 ...
Illigmann, Astrid   +4 more
openaire   +3 more sources

SpxA1 and SpxA2 act coordinately to fine-tune stress responses and virulence in Streptococcus pyogenes [PDF]

open access: yes, 2017
SpxA is a unique transcriptional regulator highly conserved among members of the phylum Firmicutes that binds RNA polymerase and can act as an antiactivator. Why some Firmicutes members have two highly similar SpxA paralogs is not understood.
Gary C. Port   +4 more
core   +7 more sources

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