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.
| Published in | Computational Biology and Bioinformatics (Volume 5, Issue 3) |
| DOI | 10.11648/j.cbb.20170503.11 |
| Page(s) | 27-35 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
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Copyright © The Author(s), 2017. Published by Science Publishing Group |
Proteolysis, Tricorn Protease, Homologs, In Silico
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APA Style
Florence Ng’ong’a, Steven Nyanjom, Fred Wamunyokoli. (2017). In Silico Analysis of Occurrence of Tricorn Protease and Its Homologs. Computational Biology and Bioinformatics, 5(3), 27-35. https://doi.org/10.11648/j.cbb.20170503.11
ACS Style
Florence Ng’ong’a; Steven Nyanjom; Fred Wamunyokoli. In Silico Analysis of Occurrence of Tricorn Protease and Its Homologs. Comput. Biol. Bioinform. 2017, 5(3), 27-35. doi: 10.11648/j.cbb.20170503.11
AMA Style
Florence Ng’ong’a, Steven Nyanjom, Fred Wamunyokoli. In Silico Analysis of Occurrence of Tricorn Protease and Its Homologs. Comput Biol Bioinform. 2017;5(3):27-35. doi: 10.11648/j.cbb.20170503.11
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Download@article{10.11648/j.cbb.20170503.11,
author = {Florence Ng’ong’a and Steven Nyanjom and Fred Wamunyokoli},
title = {In Silico Analysis of Occurrence of Tricorn Protease and Its Homologs},
journal = {Computational Biology and Bioinformatics},
volume = {5},
number = {3},
pages = {27-35},
doi = {10.11648/j.cbb.20170503.11},
url = {https://doi.org/10.11648/j.cbb.20170503.11},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.cbb.20170503.11},
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.},
year = {2017}
}
TY - JOUR T1 - In Silico Analysis of Occurrence of Tricorn Protease and Its Homologs AU - Florence Ng’ong’a AU - Steven Nyanjom AU - Fred Wamunyokoli Y1 - 2017/08/15 PY - 2017 N1 - https://doi.org/10.11648/j.cbb.20170503.11 DO - 10.11648/j.cbb.20170503.11 T2 - Computational Biology and Bioinformatics JF - Computational Biology and Bioinformatics JO - Computational Biology and Bioinformatics SP - 27 EP - 35 PB - Science Publishing Group SN - 2330-8281 UR - https://doi.org/10.11648/j.cbb.20170503.11 AB - 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. VL - 5 IS - 3 ER -
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