Results 171 to 180 of about 17,783 (200)

Effect of Clp protease from Corynebacterium glutamicum on heterologous protein expression

Protein Expression and Purification, 2022
The protease present in a host may reduce the yield and biological activity of heterologous proteins. In this study, we used protease overexpression and deletion strategies to examine the effect of the Clp protease system in Corynebacterium glutamicum on the recombinant protein and to produce a highly efficient heterologous protein expression host.
Xiuxia, Liu, Lihong, Meng, Xinyue, Wang, Yankun, Yang, Zhonghu, Bai   +4 more
openaire   +4 more sources

Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases

Nature Reviews Microbiology, 2009
Members of the AAA+ protein superfamily contribute to many diverse aspects of protein homeostasis in prokaryotic cells. As a fundamental component of numerous proteolytic machines in bacteria, AAA+ proteins play a crucial part not only in general protein quality control but also in the regulation of developmental programmes, through the controlled ...
Kirstein, Janine., Molière, Noël., Dougan, David., Turgay, Kürşad.   +3 more
openaire   +4 more sources

Tagging proteins for the Clp protease

Nature Reviews Microbiology, 2016
Katharine H Wrighton
openaire   +3 more sources

Clp chaperone–proteases: structure and function

Research in Microbiology, 2009
Clp proteases are the most widespread energy-dependent proteases in bacteria. Their two-component architecture of protease core and ATPase rings results in an inventory of several Clp protease complexes that often coexist. Here, we present insights into Clp protease function, from their assembly to substrate recruitment and processing, and how this is ...
Wolfgang, Kress, Zeljka, Maglica, Eilika, Weber-Ban   +2 more
  +6 more sources

Clp protease complexes and their diversity in chloroplasts

Planta, 1998
The Clp proteases represent a large, ancient ATP-dependent protease family which in higher plants is known to be located in chloroplasts. The soluble, presumably multisubunit, enzyme of the organelle stroma is of dual genetic origin. It consists of a nuclear-encoded, regulatory subunit ClpC, which is an ATPase, and a plastid-encoded proteolytic subunit
A, Sokolenko, S, Lerbs-Mache, L, Altschmied, R G, Herrmann   +3 more
openaire   +2 more sources

ATP-promoted interaction between Clp A and Clp P in activation of Clp protease from Escherichia coli

Biochemical Society Transactions, 1991
Summary Clp protease is a high relative molecular mass, ATP-dependent protease found in the cytoplasm of Escherichia coli. Clp protease is composed of two protein components, Clp A, which has ATPase activity, and Clp P, which has the proteolytic active site and is activated by Clp A in the presence of ATP.
openaire   +2 more sources

Uvr motifs regulate the chloroplast Clp chaperone–protease system

Trends in Plant Science
Chloroplast proteostasis relies on diverse proteases, including the essential Clp chaperone-protease system. Two chloroplast ClpC AAA+ chaperones and the plant-specific adaptor ClpF contain an Uvr motif with predicted coiled-coiled structures implicated in protein-protein interactions.
Marissa Y. Annis, Claire M. Ravenburg, Klaas J. van Wijk   +2 more
openaire   +2 more sources

ATP-Dependent association between subunits of Clp protease in pea chloroplasts

Planta, 2001
The chloroplast ATP-dependent Clp protease (EC 3.4.21.92) is composed of the proteolytic subunit ClpP and the regulatory ATPase, ClpC. Although both subunits are found in the stroma, the interaction between the two is dynamic. When immunoprecipitation with antibodies against ClpC was performed on stroma from dark-adapted pea (Pisum sativum L.
T, Halperin, O, Ostersetzer, Z, Adam
openaire   +2 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   +1 more source

Protease Ti (Clp), a multi-component ATP-dependent protease in Escherichia coli.

Biological chemistry, 1997
The ATP-dependent protease Ti(Clp) consists of two different multimeric components: ClpA containing ATP-cleaving sites and ClpP, with serine active sites for proteolysis. Here we summarize the most recent results on the structure and function of protease Ti.
C H, Chung, J H, Seol, M S, Kang
openaire   +1 more source