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Isolation and characterization of type I signal peptidase of different malaria parasites

Type I signal peptidases are important membrane-bound serine proteases responsible for the cleavage of the signal peptide of the proteins. These enzymes are unique serine proteases that carry out catalysis using a serine/lysine catalytic dyad. In the present study, we report the isolation of type I... Full description

Journal Title: Journal of Biomedicine and Biotechnology 2005, Vol.2005 (4), p.301-309
Main Author: Sharma, Sutikshan
Other Authors: Pradhan, Arun , Chauhan, Virander S , Tuteja, Renu
Format: Electronic Article Electronic Article
Language: English
Subjects:
Quelle: Alma/SFX Local Collection
Publisher: United States: Hindawi Limited
ID: ISSN: 1110-7243
Link: https://www.ncbi.nlm.nih.gov/pubmed/16489263
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title: Isolation and characterization of type I signal peptidase of different malaria parasites
format: Article
creator:
  • Sharma, Sutikshan
  • Pradhan, Arun
  • Chauhan, Virander S
  • Tuteja, Renu
subjects:
  • Article Subject
  • Biotechnology
  • Escherichia coli
  • Malaria
  • Medicine
  • Parasites
  • parasitic diseases
  • Plasmodium falciparum
  • Plasmodium knowlesi
  • Plasmodium yoelii
  • Proteases
  • Research Article
ispartof: Journal of Biomedicine and Biotechnology, 2005, Vol.2005 (4), p.301-309
description: Type I signal peptidases are important membrane-bound serine proteases responsible for the cleavage of the signal peptide of the proteins. These enzymes are unique serine proteases that carry out catalysis using a serine/lysine catalytic dyad. In the present study, we report the isolation of type I signal peptidase from the malaria parasites Plasmodium falciparum, Plasmodium knowlesi, and Plasmodium yoelii and some characterization of type I signal peptidase of Plasmodium falciparum. We show that these enzymes are homologous to signal peptidases from various sources and also contain the conserved boxes present in other type I signal peptidases. The type I signal peptidase from P falciparum is an intron-less and a single-copy gene. The results also show that the enzyme from Plasmodium falciparum is subject to self-cleavage and it has been demonstrated to possess type I signal peptidase activity in E coli preprotein processing in vivo by complementation assay. This study will be helpful in understanding one of the important metabolic pathways "the secretory pathway" in the parasite and should make an important contribution in understanding the complex process of protein targeting in the parasite.
language: eng
source: Alma/SFX Local Collection
identifier: ISSN: 1110-7243
fulltext: fulltext
issn:
  • 1110-7243
  • 1110-7251
url: Link


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descriptionType I signal peptidases are important membrane-bound serine proteases responsible for the cleavage of the signal peptide of the proteins. These enzymes are unique serine proteases that carry out catalysis using a serine/lysine catalytic dyad. In the present study, we report the isolation of type I signal peptidase from the malaria parasites Plasmodium falciparum, Plasmodium knowlesi, and Plasmodium yoelii and some characterization of type I signal peptidase of Plasmodium falciparum. We show that these enzymes are homologous to signal peptidases from various sources and also contain the conserved boxes present in other type I signal peptidases. The type I signal peptidase from P falciparum is an intron-less and a single-copy gene. The results also show that the enzyme from Plasmodium falciparum is subject to self-cleavage and it has been demonstrated to possess type I signal peptidase activity in E coli preprotein processing in vivo by complementation assay. This study will be helpful in understanding one of the important metabolic pathways "the secretory pathway" in the parasite and should make an important contribution in understanding the complex process of protein targeting in the parasite.
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subjectArticle Subject ; Biotechnology ; Escherichia coli ; Malaria ; Medicine ; Parasites ; parasitic diseases ; Plasmodium falciparum ; Plasmodium knowlesi ; Plasmodium yoelii ; Proteases ; Research Article
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abstractType I signal peptidases are important membrane-bound serine proteases responsible for the cleavage of the signal peptide of the proteins. These enzymes are unique serine proteases that carry out catalysis using a serine/lysine catalytic dyad. In the present study, we report the isolation of type I signal peptidase from the malaria parasites Plasmodium falciparum, Plasmodium knowlesi, and Plasmodium yoelii and some characterization of type I signal peptidase of Plasmodium falciparum. We show that these enzymes are homologous to signal peptidases from various sources and also contain the conserved boxes present in other type I signal peptidases. The type I signal peptidase from P falciparum is an intron-less and a single-copy gene. The results also show that the enzyme from Plasmodium falciparum is subject to self-cleavage and it has been demonstrated to possess type I signal peptidase activity in E coli preprotein processing in vivo by complementation assay. This study will be helpful in understanding one of the important metabolic pathways "the secretory pathway" in the parasite and should make an important contribution in understanding the complex process of protein targeting in the parasite.
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