Archaeal proteasomes and other regulatory proteases

Maupin-Furlow, Julie A.; Gil, Malgorzata A; Humbard, Matthew A.; Kirkland, P. Aaron; Li, Wei; Reuter, Christopher J.; Wright, Andrew Martin

doi:10.1016/j.mib.2005.10.005

Cited by 39 publications

(34 citation statements)

References 56 publications

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“…In bacteria several ATP-dependent proteases, e.g., soluble Lon, ClpAP, ClpXP, HslUV (Sauer et al, 2004;Wickner et al, 1999), as well as membrane-bound FtsH (Ito and Akiyama, 2005) seem to work in parallel. Archaea use the soluble PAN-proteasome (Wilson et al, 2000;Zwickl et al, 1999), and VAT-proteasome proteolytic systems (Gerega et al, 2005), as well as the membrane-bound Lon protease (Besche et al, 2004) for energy-dependent protein degradation (see recent review by Maupin-Furlow and colleagues (Maupin-Furlow et al, 2005)). …”

Section: Introductionmentioning

confidence: 99%

Functional and structural characterization of the Methanosarcina mazei proteasome and PAN complexes

Medalia

Sharon

Martínez‐Arias

et al. 2006

Journal of Structural Biology

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Section: Introductionmentioning

confidence: 99%

Functional and structural characterization of the Methanosarcina mazei proteasome and PAN complexes

Medalia

Sharon

Martínez‐Arias

et al. 2006

Journal of Structural Biology

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“…Lon protease was first identified in Escherichia coli (58), and Lon-homologous proteins have been further identified in a wide range of living organisms, including not only eubacteria but also archaea (42), Saccharomyces cerevisiae (65)(66)(67), plants (3,34,51), and animals (7,68). Lon protease is an ATP-and Mg 2ϩ -dependent protease belonging to the superfamily of AAA ϩ proteins (ATPases associated with different cellular activities) (43,45).…”

mentioning

confidence: 99%

Lon Protease of Azorhizobium caulinodans ORS571 Is Required for Suppression of reb Gene Expression

Nakajima

Aono

Tsukada

et al. 2012

Appl Environ Microbiol

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ABSTRACTBacterial Lon proteases play important roles in a variety of biological processes in addition to housekeeping functions. In this study, we focused on the Lon protease ofAzorhizobium caulinodans, which can fix nitrogen both during free-living growth and in stem nodules of the legumeSesbania rostrata. The nitrogen fixation activity of anA. caulinodanslonmutant in the free-living state was not significantly different from that of the wild-type strain. However, the stem nodules formed by thelonmutant showed little or no nitrogen fixation activity. By microscopic analyses, two kinds of host cells were observed in the stem nodules formed by thelonmutant. One type has shrunken host cells containing a high density of bacteria, and the other type has oval or elongated host cells containing a low density or no bacteria. This phenotype is similar to apraRmutant highly expressing therebgenes. Quantitative reverse transcription-PCR analyses revealed thatrebgenes were also highly expressed in thelonmutant. Furthermore, alon rebdouble mutant formed stem nodules showing higher nitrogen fixation activity than thelonmutant, and shrunken host cells were not observed in these stem nodules. These results suggest that Lon protease is required to suppress the expression of therebgenes and that high expression ofrebgenes in part causes aberrance in theA. caulinodans-S. rostratasymbiosis. In addition to the suppression ofrebgenes, it was found that Lon protease was involved in the regulation of exopolysaccharide production and autoagglutination of bacterial cells.

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“…Some of them present a broad specificity, and are able to bind to a variety of substrates despite the high degree of precision in the alignment of the catalytic residues involved on the peptide bond cleavage (i.e., trypsin) (Perona and Craik, 1995;Gillmor et al, 1997;Maupin-Furlow et al, 2005;Diamond, 2007). On the other hand, other proteases such as Urokinase-type plasminogen activator (U-pA) are more specific and recognize only a limited number of physiologic molecules (Diamond, 2007, Wensing et al, 2010.…”

Section: Introductionmentioning

confidence: 99%

“…Proteases catalysis can be started within a polypeptide chain (endoprotease activity) or from amino or carboxyl ends (exopeptidase activity) (Perona and Craik, 1995;Gillmor et al, 1997;Sajid and Mckerrow, 2002;Garcia-Touchard et al, 2005;Maupin-Furlow et al, 2005;Diamond, 2007). Thus, the proteases structure reflects their intringly mechanisms, which determines their proteolytic activity and specificity.…”

Section: Introductionmentioning

confidence: 99%

Looking at the proteases from a simple perspective

Castro

Abreu

Geraldo

et al. 2011

J of Molecular Recognition

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Proteases have received enormous interest from the research and medical communities because of their significant roles in several human diseases. Some examples include the involvement of thrombin in thrombosis, HIV-1 protease in Acquired Immune Deficiency Syndrome, cruzain in Trypanosoma cruzi infection, and membrane-type 1 matrix metalloproteinase in tumor invasion and metastasis. Many efforts has been undertaken to design effective inhibitors featuring potent inhibitory activity, specificity, and metabolic stability to those proteases involved in such pathologies. Protease inhibitors usually target the active site, but some of them act by other inhibitory mechanisms. The understanding of the structure-function relationships of proteases and inhibitors has an impact on new inhibitor drugs designing. In this paper, the structures of four proteases (thrombin, HIV-protease, cruzain, and a matrix metalloproteinase) are briefly reviewed, and used as examples of the importance of proteases for the development of new treatment strategies, leading to a longer and healthier life.

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Archaeal proteasomes and other regulatory proteases

Cited by 39 publications

References 56 publications

Functional and structural characterization of the Methanosarcina mazei proteasome and PAN complexes

Functional and structural characterization of the Methanosarcina mazei proteasome and PAN complexes

Lon Protease of Azorhizobium caulinodans ORS571 Is Required for Suppression of reb Gene Expression

Looking at the proteases from a simple perspective

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