Crystal Structure of TET Protease Reveals Complementary Protein Degradation Pathways in Prokaryotes

Borissenko, Ljudmila; Groll, M.

doi:10.1016/j.jmb.2004.12.056

Cited by 62 publications

(125 citation statements)

References 35 publications

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“…The typical TET dodecahedral quaternary structure was initially described in archaea (18,22,23). It was also found in bacteria (24), and recently, the crystallographic structure of bovine and human tetrahedral aspartylaminopeptidases have revealed that the TET complexes are also present in eukaryotic cells (25,26).…”

mentioning

confidence: 94%

“…Because of their cooperative action, the archaeal TET peptidases can be designated as a "peptidasome" involved in the destruction of a vast variety of polypeptides. It has been suggested that, in peptide-fermenting organisms, the TET system plays an important role in the energy metabolism (19) or in the intracellular protein degradation by hydrolyzing the peptides produced by the proteasome endopeptidase activity (23). In addition, the TET peptidases could play more specific physiological roles as they can cleave physiologically relevant peptides.…”

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confidence: 99%

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Pyrococcus horikoshii TET2 Peptidase Assembling Process and Associated Functional Regulation

Appolaire¹,

Rosenbaum²,

Durá³

et al. 2013

Journal of Biological Chemistry

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Background: TET aminopeptidases are 12-subunit complexes present in the three domains of life and are involved in important biological functions. Results: The TET assembling process has been characterized. The oligomerization triggers TET activity toward large polypeptidic substrates. Conclusion:The assembling of TET is a controlled process and regulates its activity in vivo. Significance: This work provides a new example of peptidase regulation driven by self-oligomerization.

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confidence: 94%

mentioning

confidence: 99%

Pyrococcus horikoshii TET2 Peptidase Assembling Process and Associated Functional Regulation

Appolaire¹,

Rosenbaum²,

Durá³

et al. 2013

Journal of Biological Chemistry

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“…The identification criteria used in this study did not find tricorn protease or its homologs in methanogens, desulforococales, nanoarchaeota and korarchaeota which have been shown to have complementary pathways [9]. However, this study predicts the existence of tricorn protease/ tricorn protease homologs in all the bacterial phyla with complete similar functional domains (beta-propeller, PDZ and catalytic domains).…”

Section: Discussionmentioning

confidence: 71%

“…Indeed, tetrahedral aminopeptidase (TET) has been shown to be a complementary protein degradation machinery to tricorn protease in Pyrococcus horikoshii and it degrades peptides to free amino acids [9]. In eukaryotes, tripeptidyl peptidase II (TPP II) is a tricorn protease functional analog, and has been shown to act downstream of the proteasome [10] [11] [12], where it is implicated in peptide processing of MHC class I antigens [13] [14].…”

Section: Introductionmentioning

confidence: 99%

<i>In Silico</i> Analysis of Occurrence of Tricorn Protease and Its Homologs

Ng’ong’a¹

2017

CBB

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Abstract:Tricorn protease is an archaeal protease acting downstream of the proteasome and together with its interacting aminopeptidases, degrades oligopeptides to free amino acids thus playing an important role in protein turnover. This study reports a wide distribution of tricorn protease and its homologs in archaea and bacteria. The homologs were identified through a combination of PSI-BLAST, orthology clustering and domain predictions. Functionally important sites were identified through multiple sequence alignment conducted by MAFFT v. 7. The aligned sequences were used to predict the phylogenetic relationship of tricorn protease and its homologs using MEGA v. 7. The functional associations of tricorn protease were predicted through STRING network v.10.0. This study identified several tricorn protease homologs in archaea and in all the bacterial phyla complete with β-propeller, PDZ and catalytic domains. However, in eukaryotes, tricorn protease-like homologs seemed limited to viridiplantae, stramenopile and in a basal metazoa and were classified as non-peptidase homologs with unknown functions. Conserved domain architecture retrieval revealed detectable homology of tricorn protease C-terminal half with the carboxyl-terminal proteases with similar PDZ domains. Therefore, this study predicts functional conservation of tricorn core catalytic domain in prokaryotes and given its role in cellular functions, targeting this protein or its functional homologs in prokaryotic pathogens could lead to development of alternative therapeutic agents.

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“…Studies have also shown that tricorn protease is patchily distributed and other archaeon such as Desulforococcales, example Pyrolobus, Desulforococcus lack tricorn protease but have tetrahedral aminopeptidase (TET) which also acts downstream of the proteasome assumes the role of tricorn protease (Borissenko & Groll 2005). …”

Section: Issn (Online): 2319-7064mentioning

confidence: 99%

A Functional Comparison of the Archaeon Tricorn Protease and Selected Serine Proteases from Trypanosoma brucei brucei

2016

IJSR

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Trypanosomes are protozoan parasites causing African trypanosomiasis, a neglected tropical disease in Africa affecting humans and animals. Current control methods have focused on the use of drugs which have adverse effects and develop resistance and with no available conventional vaccine. Proteolysis is a key process in trypanosome survival in the mammalian host hence identification of other parasitic factors would lead to the development of new chemotherapeutic agents. This study investigated archaeon tricorn protease functional analogs in Trypanosoma brucei brucei through bioinformatics approaches. The protein sequences were retrieved from NCBI (http://www.ncbi.nlm.nih.gov/protein/) and position specific iterated basic local sequence alignment (PSI-BLAST) was performed using default parameters to determine patterns of conservation which aid in the recognition of distant similarities. The 3D models of the putative proteins were constructed using T. acidophilum tricorn protease. The constructed models were analyzed based on percentage identity, e-value and bit-score. Structural alignment was done using MATRAS (http://strcomp.protein.osaka-u.ac.jp/matras/) and PyMOL Molecular Graphics System, Version 1.8 Schrödinger, LLC (https://www.pymol.org/) was used for viewing and structural analysis. The bioinformatics analysis revealed similarities in the catalytic core elements as well as the beta sheets serving as substrate entry and exit route to and from the catalytic chamber. Therefore, based on these similarities, this study reports the identification tricorn protease functional analogs in Trypanosoma brucei brucei.

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Crystal Structure of TET Protease Reveals Complementary Protein Degradation Pathways in Prokaryotes

Cited by 62 publications

References 35 publications

Pyrococcus horikoshii TET2 Peptidase Assembling Process and Associated Functional Regulation

Pyrococcus horikoshii TET2 Peptidase Assembling Process and Associated Functional Regulation

<i>In Silico</i> Analysis of Occurrence of Tricorn Protease and Its Homologs

A Functional Comparison of the Archaeon Tricorn Protease and Selected Serine Proteases from Trypanosoma brucei brucei

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Crystal Structure of TET Protease Reveals Complementary Protein Degradation Pathways in Prokaryotes

Cited by 62 publications

References 35 publications

Pyrococcus horikoshii TET2 Peptidase Assembling Process and Associated Functional Regulation

Pyrococcus horikoshii TET2 Peptidase Assembling Process and Associated Functional Regulation

&lt;i&gt;In Silico&lt;/i&gt; Analysis of Occurrence of Tricorn Protease and Its Homologs

A Functional Comparison of the Archaeon Tricorn Protease and Selected Serine Proteases from Trypanosoma brucei brucei

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<i>In Silico</i> Analysis of Occurrence of Tricorn Protease and Its Homologs