Literature DB >> 19772918

Regulation and quality control by Lon-dependent proteolysis.

Laurence Van Melderen1, Abram Aertsen.   

Abstract

After their first discovery in Escherichia coli, Lon homologues were found to be widely distributed among prokaryotes to eukaryotes. The ATP-dependent Lon protease belongs to the AAA(+) (ATPases associated with a variety of cellular activities) superfamily, and is involved in both general quality control by degrading abnormal proteins and in the specific control of several regulatory proteins. As such, this enzyme has a pivotal role in quality control and cellular physiology. This review focuses on mechanisms of degradation both from the protease and substrate points of view, and discusses the role of Lon in global regulation, stress response and virulence.

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Year:  2009        PMID: 19772918     DOI: 10.1016/j.resmic.2009.08.021

Source DB:  PubMed          Journal:  Res Microbiol        ISSN: 0923-2508            Impact factor:   3.992


  41 in total

Review 1.  Post-transcriptional global regulation by CsrA in bacteria.

Authors:  Johan Timmermans; Laurence Van Melderen
Journal:  Cell Mol Life Sci       Date:  2010-05-06       Impact factor: 9.261

2.  Microbial metabolic potential for carbon degradation and nutrient (nitrogen and phosphorus) acquisition in an ombrotrophic peatland.

Authors:  Xueju Lin; Malak M Tfaily; Stefan J Green; J Megan Steinweg; Patrick Chanton; Aopeau Imvittaya; Jeffrey P Chanton; William Cooper; Christopher Schadt; Joel E Kostka
Journal:  Appl Environ Microbiol       Date:  2014-03-28       Impact factor: 4.792

3.  Two proteases, trypsin domain-containing 1 (Tysnd1) and peroxisomal lon protease (PsLon), cooperatively regulate fatty acid β-oxidation in peroxisomal matrix.

Authors:  Kanji Okumoto; Yukari Kametani; Yukio Fujiki
Journal:  J Biol Chem       Date:  2011-10-14       Impact factor: 5.157

4.  Cellular filamentation after sublethal high-pressure shock in Escherichia coli K12 is Mrr dependent.

Authors:  Anirban Ghosh; Abram Aertsen
Journal:  Curr Microbiol       Date:  2013-09-04       Impact factor: 2.188

5.  A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis.

Authors:  Wataru Nishii; Mutsuko Kukimoto-Niino; Takaho Terada; Mikako Shirouzu; Tomonari Muramatsu; Masaki Kojima; Hiroshi Kihara; Shigeyuki Yokoyama
Journal:  Nat Chem Biol       Date:  2014-11-10       Impact factor: 15.040

6.  Enzyme regulation: a thiol switch opens the gate.

Authors:  Haike Antelmann
Journal:  Nat Chem Biol       Date:  2014-11-10       Impact factor: 15.040

7.  Crystal structure of the N domain of Lon protease from Mycobacterium avium complex.

Authors:  Xiaoyan Chen; Shijun Zhang; Fangkai Bi; Chenyun Guo; Liubin Feng; Huilin Wang; Hongwei Yao; Donghai Lin
Journal:  Protein Sci       Date:  2019-09       Impact factor: 6.725

8.  Identification of Burkholderia cenocepacia strain H111 virulence factors using nonmammalian infection hosts.

Authors:  Stephan Schwager; Kirsty Agnoli; Manuela Köthe; Friederike Feldmann; Michael Givskov; Aurelien Carlier; Leo Eberl
Journal:  Infect Immun       Date:  2012-10-22       Impact factor: 3.441

9.  A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli.

Authors:  Kai Westphal; Sina Langklotz; Nikolas Thomanek; Franz Narberhaus
Journal:  J Biol Chem       Date:  2012-10-22       Impact factor: 5.157

10.  The Lon protease-like domain in the bacterial RecA paralog RadA is required for DNA binding and repair.

Authors:  Masao Inoue; Kenji Fukui; Yuki Fujii; Noriko Nakagawa; Takato Yano; Seiki Kuramitsu; Ryoji Masui
Journal:  J Biol Chem       Date:  2017-04-21       Impact factor: 5.157

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