Native Electrophoresis-Coupled Activity Assays Reveal Catalytically-Active Protein Aggregates of Escherichia coli β-Glucuronidase.
β-glucuronidase is found as a functional homotetramer in a variety of organisms, including humans and other animals, as well as a number of bacteria. This enzyme is important in these organisms, catalyzing the hydrolytic removal of a glucuronide moiety from substrate molecules. This process serves t...
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doaj-aca65e07fd854645a5af48d6c719b1a42020-11-25T02:33:33ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01106e013026910.1371/journal.pone.0130269Native Electrophoresis-Coupled Activity Assays Reveal Catalytically-Active Protein Aggregates of Escherichia coli β-Glucuronidase.Gina G BurchettCharles G FolsomKimberly T Laneβ-glucuronidase is found as a functional homotetramer in a variety of organisms, including humans and other animals, as well as a number of bacteria. This enzyme is important in these organisms, catalyzing the hydrolytic removal of a glucuronide moiety from substrate molecules. This process serves to break down sugar conjugates in animals and provide sugars for metabolism in bacteria. While β-glucuronidase is primarily found as a homotetramer, previous studies have indicated that the human form of the protein is also catalytically active as a dimer. Here we present evidence for not only an active dimer of the E. coli form of the protein, but also for several larger active complexes, including an octomer and a 16-mer. Additionally, we propose a model for the structures of these large complexes, based on computationally-derived molecular modeling studies. These structures may have application in the study of human disease, as several diseases have been associated with the aggregation of proteins.http://europepmc.org/articles/PMC4484804?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Gina G Burchett Charles G Folsom Kimberly T Lane |
spellingShingle |
Gina G Burchett Charles G Folsom Kimberly T Lane Native Electrophoresis-Coupled Activity Assays Reveal Catalytically-Active Protein Aggregates of Escherichia coli β-Glucuronidase. PLoS ONE |
author_facet |
Gina G Burchett Charles G Folsom Kimberly T Lane |
author_sort |
Gina G Burchett |
title |
Native Electrophoresis-Coupled Activity Assays Reveal Catalytically-Active Protein Aggregates of Escherichia coli β-Glucuronidase. |
title_short |
Native Electrophoresis-Coupled Activity Assays Reveal Catalytically-Active Protein Aggregates of Escherichia coli β-Glucuronidase. |
title_full |
Native Electrophoresis-Coupled Activity Assays Reveal Catalytically-Active Protein Aggregates of Escherichia coli β-Glucuronidase. |
title_fullStr |
Native Electrophoresis-Coupled Activity Assays Reveal Catalytically-Active Protein Aggregates of Escherichia coli β-Glucuronidase. |
title_full_unstemmed |
Native Electrophoresis-Coupled Activity Assays Reveal Catalytically-Active Protein Aggregates of Escherichia coli β-Glucuronidase. |
title_sort |
native electrophoresis-coupled activity assays reveal catalytically-active protein aggregates of escherichia coli β-glucuronidase. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2015-01-01 |
description |
β-glucuronidase is found as a functional homotetramer in a variety of organisms, including humans and other animals, as well as a number of bacteria. This enzyme is important in these organisms, catalyzing the hydrolytic removal of a glucuronide moiety from substrate molecules. This process serves to break down sugar conjugates in animals and provide sugars for metabolism in bacteria. While β-glucuronidase is primarily found as a homotetramer, previous studies have indicated that the human form of the protein is also catalytically active as a dimer. Here we present evidence for not only an active dimer of the E. coli form of the protein, but also for several larger active complexes, including an octomer and a 16-mer. Additionally, we propose a model for the structures of these large complexes, based on computationally-derived molecular modeling studies. These structures may have application in the study of human disease, as several diseases have been associated with the aggregation of proteins. |
url |
http://europepmc.org/articles/PMC4484804?pdf=render |
work_keys_str_mv |
AT ginagburchett nativeelectrophoresiscoupledactivityassaysrevealcatalyticallyactiveproteinaggregatesofescherichiacolibglucuronidase AT charlesgfolsom nativeelectrophoresiscoupledactivityassaysrevealcatalyticallyactiveproteinaggregatesofescherichiacolibglucuronidase AT kimberlytlane nativeelectrophoresiscoupledactivityassaysrevealcatalyticallyactiveproteinaggregatesofescherichiacolibglucuronidase |
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