Literature DB >> 15606774

Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains.

Tatyana V Rotanova1, Edward E Melnikov, Anna G Khalatova, Oksana V Makhovskaya, Istvan Botos, Alexander Wlodawer, Alla Gustchina.   

Abstract

ATP-dependent Lon proteases belong to the superfamily of AAA+ proteins. Until recently, the identity of the residues involved in their proteolytic active sites was not elucidated. However, the putative catalytic Ser-Lys dyad was recently suggested through sequence comparison of more than 100 Lon proteases from various sources. The presence of the catalytic dyad was experimentally confirmed by site-directed mutagenesis of the Escherichia coli Lon protease and by determination of the crystal structure of its proteolytic domain. Furthermore, this extensive sequence analysis allowed the definition of two subfamilies of Lon proteases, LonA and LonB, based on the consensus sequences in the active sites of their proteolytic domains. These differences strictly associate with the specific characteristics of their AAA+ modules, as well as with the presence or absence of an N-terminal domain.

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Year:  2004        PMID: 15606774     DOI: 10.1111/j.1432-1033.2004.04452.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  28 in total

1.  Structure of the N-terminal fragment of Escherichia coli Lon protease.

Authors:  Mi Li; Alla Gustchina; Fatima S Rasulova; Edward E Melnikov; Michael R Maurizi; Tatyana V Rotanova; Zbigniew Dauter; Alexander Wlodawer
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2010-07-09

Review 2.  Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.

Authors:  Tatyana V Rotanova; Istvan Botos; Edward E Melnikov; Fatima Rasulova; Alla Gustchina; Michael R Maurizi; Alexander Wlodawer
Journal:  Protein Sci       Date:  2006-08       Impact factor: 6.725

3.  Recognition of misfolded proteins by Lon, a AAA(+) protease.

Authors:  Eyal Gur; Robert T Sauer
Journal:  Genes Dev       Date:  2008-08-15       Impact factor: 11.361

Review 4.  Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments.

Authors:  Kenji Nishimura; Yusuke Kato; Wataru Sakamoto
Journal:  Plant Physiol       Date:  2016-06-10       Impact factor: 8.340

Review 5.  Multitasking in the mitochondrion by the ATP-dependent Lon protease.

Authors:  Sundararajan Venkatesh; Jae Lee; Kamalendra Singh; Irene Lee; Carolyn K Suzuki
Journal:  Biochim Biophys Acta       Date:  2011-11-18

6.  Crystal structure of the N-terminal domain of E. coli Lon protease.

Authors:  Mi Li; Fatima Rasulova; Edward E Melnikov; Tatyana V Rotanova; Alla Gustchina; Michael R Maurizi; Alexander Wlodawer
Journal:  Protein Sci       Date:  2005-09-30       Impact factor: 6.725

7.  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

8.  Characterization of three putative Lon proteases of Thermus thermophilus HB27 and use of their defective mutants as hosts for production of heterologous proteins.

Authors:  Tomoko Maehara; Takayuki Hoshino; Akira Nakamura
Journal:  Extremophiles       Date:  2007-12-22       Impact factor: 2.395

Review 9.  Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates.

Authors:  Irene Lee; Carolyn K Suzuki
Journal:  Biochim Biophys Acta       Date:  2008-03-05

10.  Negative regulation of quorum-sensing systems in Pseudomonas aeruginosa by ATP-dependent Lon protease.

Authors:  Akiko Takaya; Fumiaki Tabuchi; Hiroko Tsuchiya; Emiko Isogai; Tomoko Yamamoto
Journal:  J Bacteriol       Date:  2008-04-11       Impact factor: 3.490

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