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Large-Size Subunit Catalases Are Chimeric Proteins: A H(2)O(2) Selecting Domain with Catalase Activity Fused to a Hsp31-Derived Domain Conferring Protein Stability and Chaperone Activity

Bacterial and fungal large-size subunit catalases (LSCs) are like small-size subunit catalases (SSCs) but have an additional C-terminal domain (CT). The catalytic domain is conserved at both primary sequence and structural levels and its amino acid composition is optimized to select H(2)O(2) over wa...

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Autores principales: Hansberg, Wilhelm, Nava-Ramírez, Teresa, Rangel-Silva, Pablo, Díaz-Vilchis, Adelaida, Mendoza-Oliva, Aydé
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9137513/
https://www.ncbi.nlm.nih.gov/pubmed/35624843
http://dx.doi.org/10.3390/antiox11050979
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author Hansberg, Wilhelm
Nava-Ramírez, Teresa
Rangel-Silva, Pablo
Díaz-Vilchis, Adelaida
Mendoza-Oliva, Aydé
author_facet Hansberg, Wilhelm
Nava-Ramírez, Teresa
Rangel-Silva, Pablo
Díaz-Vilchis, Adelaida
Mendoza-Oliva, Aydé
author_sort Hansberg, Wilhelm
collection PubMed
description Bacterial and fungal large-size subunit catalases (LSCs) are like small-size subunit catalases (SSCs) but have an additional C-terminal domain (CT). The catalytic domain is conserved at both primary sequence and structural levels and its amino acid composition is optimized to select H(2)O(2) over water. The CT is structurally conserved, has an amino acid composition similar to very stable proteins, confers high stability to LSCs, and has independent molecular chaperone activity. While heat and denaturing agents increased Neurospora crassa catalase-1 (CAT-1) activity, a CAT-1 version lacking the CT (C63) was no longer activated by these agents. The addition of catalase-3 (CAT-3) CT to the CAT-1 or CAT-3 catalase domains prevented their heat denaturation in vitro. Protein structural alignments indicated CT similarity with members of the DJ-1/PfpI superfamily and the CT dimers present in LSCs constitute a new type of symmetric dimer within this superfamily. However, only the bacterial Hsp31 proteins show sequence similarity to the bacterial and fungal catalase mobile coil (MC) and are phylogenetically related to MC_CT sequences. LSCs might have originated by fusion of SSC and Hsp31 encoding genes during early bacterial diversification, conferring at the same time great stability and molecular chaperone activity to the novel catalases.
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spelling pubmed-91375132022-05-28 Large-Size Subunit Catalases Are Chimeric Proteins: A H(2)O(2) Selecting Domain with Catalase Activity Fused to a Hsp31-Derived Domain Conferring Protein Stability and Chaperone Activity Hansberg, Wilhelm Nava-Ramírez, Teresa Rangel-Silva, Pablo Díaz-Vilchis, Adelaida Mendoza-Oliva, Aydé Antioxidants (Basel) Article Bacterial and fungal large-size subunit catalases (LSCs) are like small-size subunit catalases (SSCs) but have an additional C-terminal domain (CT). The catalytic domain is conserved at both primary sequence and structural levels and its amino acid composition is optimized to select H(2)O(2) over water. The CT is structurally conserved, has an amino acid composition similar to very stable proteins, confers high stability to LSCs, and has independent molecular chaperone activity. While heat and denaturing agents increased Neurospora crassa catalase-1 (CAT-1) activity, a CAT-1 version lacking the CT (C63) was no longer activated by these agents. The addition of catalase-3 (CAT-3) CT to the CAT-1 or CAT-3 catalase domains prevented their heat denaturation in vitro. Protein structural alignments indicated CT similarity with members of the DJ-1/PfpI superfamily and the CT dimers present in LSCs constitute a new type of symmetric dimer within this superfamily. However, only the bacterial Hsp31 proteins show sequence similarity to the bacterial and fungal catalase mobile coil (MC) and are phylogenetically related to MC_CT sequences. LSCs might have originated by fusion of SSC and Hsp31 encoding genes during early bacterial diversification, conferring at the same time great stability and molecular chaperone activity to the novel catalases. MDPI 2022-05-17 /pmc/articles/PMC9137513/ /pubmed/35624843 http://dx.doi.org/10.3390/antiox11050979 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Hansberg, Wilhelm
Nava-Ramírez, Teresa
Rangel-Silva, Pablo
Díaz-Vilchis, Adelaida
Mendoza-Oliva, Aydé
Large-Size Subunit Catalases Are Chimeric Proteins: A H(2)O(2) Selecting Domain with Catalase Activity Fused to a Hsp31-Derived Domain Conferring Protein Stability and Chaperone Activity
title Large-Size Subunit Catalases Are Chimeric Proteins: A H(2)O(2) Selecting Domain with Catalase Activity Fused to a Hsp31-Derived Domain Conferring Protein Stability and Chaperone Activity
title_full Large-Size Subunit Catalases Are Chimeric Proteins: A H(2)O(2) Selecting Domain with Catalase Activity Fused to a Hsp31-Derived Domain Conferring Protein Stability and Chaperone Activity
title_fullStr Large-Size Subunit Catalases Are Chimeric Proteins: A H(2)O(2) Selecting Domain with Catalase Activity Fused to a Hsp31-Derived Domain Conferring Protein Stability and Chaperone Activity
title_full_unstemmed Large-Size Subunit Catalases Are Chimeric Proteins: A H(2)O(2) Selecting Domain with Catalase Activity Fused to a Hsp31-Derived Domain Conferring Protein Stability and Chaperone Activity
title_short Large-Size Subunit Catalases Are Chimeric Proteins: A H(2)O(2) Selecting Domain with Catalase Activity Fused to a Hsp31-Derived Domain Conferring Protein Stability and Chaperone Activity
title_sort large-size subunit catalases are chimeric proteins: a h(2)o(2) selecting domain with catalase activity fused to a hsp31-derived domain conferring protein stability and chaperone activity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9137513/
https://www.ncbi.nlm.nih.gov/pubmed/35624843
http://dx.doi.org/10.3390/antiox11050979
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