Protease I from Pyrococcus furiosus

Chang, Lara S; Hicks, Paula M; Kelly, Robert M.

doi:10.1016/s0076-6879(01)30392-0

Cited by 11 publications

(10 citation statements)

References 10 publications

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“…The other ORF exhibited highest homology of 73% with that of P. horikoshii. Carboxypeptidase Taq from Thermus aquaticus (Lee et al, 1994), Thermus thermophilus (Nagata et al, 2004), Thermococcus sp NA1 (Lee et al, 2006) and P. furiosus (Chang et al, 2001) have been characterized. Carboxypeptidase from Thermococcus sp NA1 shows broad substrate specificity which makes it a potential candidate in C-terminal sequencing.…”

Section: Carboxypeptidasesmentioning

confidence: 99%

“…The intracellular serine protease in T. kodakaraensis genome is highly homologous (83% identical) to protease I (PfpI), an internal peptidase of P. furiosus (Halio et al, 1997). PfpI, in vitro, is found in three functional forms, a trimer, a hexamer and a dodecamer (Chang et al, 2001). It appeared that it may exist as an ATP independent protease complex and behaves like proteasome.…”

Section: Intracellular Peptidasesmentioning

confidence: 99%

See 1 more Smart Citation

Proteolytic inventory of Thermococcus kodakaraensis

Rasool¹,

Rashid²,

Bashir³

et al. 2013

Afr. J. Microbiol. Res.

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Proteolysis is a very crucial process for development and survival of the cell. Genome sequence data can be employed to estimate proteolysis inventories of different organisms. In this review, we exploit genome sequence data of hyperthermophilic archaeon Thermococcus kodakaraensis to have an overview of the proteolysis in this microorganism. The overview is based on those peptidases that have been characterized, and on putative peptidases that have been identified but have yet to be characterized. In contrast to bacteria, the number of proteolytic enzymes in archaea is quite low. By analyzing the genome sequence data, we tried to establish how T. kodakaraensis maintains its life cycle and other processes by using such a small number of protein scavengers while harboring at high temperature where chances of protein denaturation are high.

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Section: Carboxypeptidasesmentioning

confidence: 99%

Section: Intracellular Peptidasesmentioning

confidence: 99%

Proteolytic inventory of Thermococcus kodakaraensis

Rasool¹,

Rashid²,

Bashir³

et al. 2013

Afr. J. Microbiol. Res.

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“…The gene encoding this subunit has putative homologs in other cells and microorganisms from the three domains of life, including M. jannaschii, B. subtilis, E. coli and Homo sapiens, but not T. maritima or Saccharomyces cerevisiae. In vitro, PfpI occurs in at least three functional forms, a trimer, a hexamer and a dodecamer, and is most active as a dodecamer (Chang et al 2001). The physiological role of PfpI is unclear, but it complements the proteasome in P. furiosus; in vitro, a synergistic relationship between the two proteases has been noted (Chang et al 2001).…”

Section: Atp-independent Proteases In Hyperthermophilesmentioning

confidence: 99%

Proteolysis in hyperthermophilic microorganisms

Ward

Shockley

Chang

et al. 2002

Archaea

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Proteases are found in every cell, where they recognize and break down unneeded or abnormal polypeptides or peptide-based nutrients within or outside the cell. Genome sequence data can be used to compare proteolytic enzyme inventories of different organisms as they relate to physiological needs for protein modification and hydrolysis. In this review, we exploit genome sequence data to compare hyperthermophilic microorganisms from the euryarchaeotal genus Pyrococcus, the crenarchaeote Sulfolobus solfataricus, and the bacterium Thermotoga maritima. An overview of the proteases in these organisms is given based on those proteases that have been characterized and on putative proteases that have been identified from genomic sequences, but have yet to be characterized. The analysis revealed both similarities and differences in the mechanisms utilized for proteolysis by each of these hyperthermophiles and indicated how these mechanisms relate to proteolysis in less thermophilic cells and organisms.

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“…Genome sequence analyses have shown that the Clp family of proteases which occur in both bacteria and eukaryotes is absent in all hyperthermophilic archaea, and that no homologue of Lon that is ubiquitous across all three domains of life could be identified in the genome of the hyperthermophilic crenarchaeon Sulfolobus solfataricus ; therefore proteases are believed to be among the genes in hyperthermophilic genomes that are still unassigned in terms of function [2]. Table 1 summarizes the intracellular proteases isolated so far from hyperthermophilic archaea [3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20] : the organisms are all Euryarchaea, except for Pyrobaculum aerophilum, Aeropyrum pernix and S. solfataricus, which belong to the Crenarchaeota kingdom. Some archaeal proteases are novel proteins.…”

Section: Introductionmentioning

confidence: 99%

“…Some archaeal proteases are novel proteins. The sequence-related cysteine proteases of Pyrococcus furiosus [8] and Pyrococcus horikoshii [13], as well as the serine prolyl endopeptidase of P. furiosus [7], have no sequence similarity to any known protease family ; the Thermococcus litoralis cysteine pyrrolidone carboxyl peptidase has no sequence or structural similarity to other members of the cysteine protease family, but it shows considerable similarities to other hydrolytic enzymes of widely differing substrate specificity and mechanism, Abbreviations used : Ac, acetyl ; AMC, 7-amido-4-methylcoumarin ; CBz, benzyloxycarbonyl ; E-64, trans-epoxysuccinyl-L-leucylamido-(4guanidino)butane ; Suc, N-succinyl. 1 To whom correspondence should be addressed (e-mail guaglia!unina.it).…”

Section: Introductionmentioning

confidence: 99%

An intracellular protease of the crenarchaeon Sulfolobus solfataricus, which has sequence similarity to eukaryotic peptidases of the CD clan

Guagliardi

Cerchia

Rossi

2002

Biochemical Journal

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We purified from crude extracts of the hyperthermophilic crenarchaeon Sulfolobus solfataricus a protease that is able to hydrolyse proteins with a pH optimum of 7.5 and a temperature optimum of 70 degrees C. Assays in the presence of classical protease inhibitors showed that the hydrolytic activity is sensitive to thiol-blocking reagents. Fluorescence assays using synthetic peptides demonstrated that the protease has a preference for cleaving glutamic acid residues. The first 12 residues of the protease match the N-terminus residues of a hypothetical protein in the S. solfataricus genome of 95 amino acids in length and calculated molecular mass of 11072 Da. The whole sequence of the protease is not related to any known protein, but it bears a segment which is highly similar to one containing the active cysteine residue in eukaryotic peptidases known as legumains. This is the first protease isolated from S. solfataricus capable of degrading native proteins effectively. Our results add to the knowledge of the intracellular proteolytic machine in hyperthermophilic micro-organisms.

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Protease I from Pyrococcus furiosus

Cited by 11 publications

References 10 publications

Proteolytic inventory of Thermococcus kodakaraensis

Proteolytic inventory of Thermococcus kodakaraensis

Proteolysis in hyperthermophilic microorganisms

An intracellular protease of the crenarchaeon Sulfolobus solfataricus, which has sequence similarity to eukaryotic peptidases of the CD clan

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