Structural and functional analysis of human HtrA3 protease and its subdomains
Abstract
Human HtrA3 protease, which induces mitochondria-mediated apoptosis, can be a tumor suppressor and a potential therapeutic target in the treatment of cancer. However, there is little information about its structure and biochemical properties. HtrA3 is composed of an N-terminal domain not required for proteolytic activity, a central serine protease domain and a C-terminal PDZ domain. HtrA3S, its short natural isoform, lacks the PDZ domain which is substituted by a stretch of 7 C-terminal amino acid residues, unique for this isoform. This paper presents the crystal structure of the HtrA3 protease domain together with the PDZ domain (ΔN-HtrA3), showing that the protein forms a trimer whose protease domains are similar to those of human HtrA1 and HtrA2. The ΔN-HtrA3 PDZ domains are placed in a position intermediate between that in the flat saucer-like HtrA1 SAXS structure and the compact pyramidal HtrA2 X-ray structure. The PDZ domain interacts closely with the LB loop of the protease domain in a way not found in other human HtrAs. ΔN-HtrA3 with the PDZ removed (ΔN-HtrA3-ΔPDZ) and an N-terminally truncated HtrA3S (ΔN-HtrA3S) were fully active at a wide range of temperatures and their substrate affinity was not impaired. This indicates that the PDZ domain is dispensablemore »
- Authors:
-
- Univ. of Gdansk (Poland). Dept. of Biochemistry.
- Argonne National Lab., Argonne, IL (United States). Midwest Center for Structural Genomics and Structural Biology Center.
- Univ. of Gdansk (Poland). Dept. of Molecular and Cellular Biology; Medical Univ. of Gdansk (Poland)
- Centro Nacional de Biotecnologia - CSIC (Spain)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institute of Health; Polish National Science Centre (NCN)
- OSTI Identifier:
- 1212403
- Grant/Contract Number:
- AC02-06CH11357
- Resource Type:
- Accepted Manuscript
- Journal Name:
- PLoS ONE
- Additional Journal Information:
- Journal Volume: 10; Journal Issue: 6; Journal ID: ISSN 1932-6203
- Publisher:
- Public Library of Science
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; proteases; crystal structure; protein structure; peptides; oligomers; serine proteases; size-exclusion chromatography; X-ray crystallography
Citation Formats
Glaza, Przemyslaw, Osipiuk, Jerzy, Wenta, Tomasz, Zurawa-Janicka, Dorota, Jarzab, Miroslaw, Lesner, Adam, Banecki, Bogdan, Skorko-Glonek, Joanna, Joachimiak, Andrzej, Lipinska, Barbara, and van Raaij, Mark J. Structural and functional analysis of human HtrA3 protease and its subdomains. United States: N. p., 2015.
Web. doi:10.1371/journal.pone.0131142.
Glaza, Przemyslaw, Osipiuk, Jerzy, Wenta, Tomasz, Zurawa-Janicka, Dorota, Jarzab, Miroslaw, Lesner, Adam, Banecki, Bogdan, Skorko-Glonek, Joanna, Joachimiak, Andrzej, Lipinska, Barbara, & van Raaij, Mark J. Structural and functional analysis of human HtrA3 protease and its subdomains. United States. https://doi.org/10.1371/journal.pone.0131142
Glaza, Przemyslaw, Osipiuk, Jerzy, Wenta, Tomasz, Zurawa-Janicka, Dorota, Jarzab, Miroslaw, Lesner, Adam, Banecki, Bogdan, Skorko-Glonek, Joanna, Joachimiak, Andrzej, Lipinska, Barbara, and van Raaij, Mark J. Thu .
"Structural and functional analysis of human HtrA3 protease and its subdomains". United States. https://doi.org/10.1371/journal.pone.0131142. https://www.osti.gov/servlets/purl/1212403.
@article{osti_1212403,
title = {Structural and functional analysis of human HtrA3 protease and its subdomains},
author = {Glaza, Przemyslaw and Osipiuk, Jerzy and Wenta, Tomasz and Zurawa-Janicka, Dorota and Jarzab, Miroslaw and Lesner, Adam and Banecki, Bogdan and Skorko-Glonek, Joanna and Joachimiak, Andrzej and Lipinska, Barbara and van Raaij, Mark J.},
abstractNote = {Human HtrA3 protease, which induces mitochondria-mediated apoptosis, can be a tumor suppressor and a potential therapeutic target in the treatment of cancer. However, there is little information about its structure and biochemical properties. HtrA3 is composed of an N-terminal domain not required for proteolytic activity, a central serine protease domain and a C-terminal PDZ domain. HtrA3S, its short natural isoform, lacks the PDZ domain which is substituted by a stretch of 7 C-terminal amino acid residues, unique for this isoform. This paper presents the crystal structure of the HtrA3 protease domain together with the PDZ domain (ΔN-HtrA3), showing that the protein forms a trimer whose protease domains are similar to those of human HtrA1 and HtrA2. The ΔN-HtrA3 PDZ domains are placed in a position intermediate between that in the flat saucer-like HtrA1 SAXS structure and the compact pyramidal HtrA2 X-ray structure. The PDZ domain interacts closely with the LB loop of the protease domain in a way not found in other human HtrAs. ΔN-HtrA3 with the PDZ removed (ΔN-HtrA3-ΔPDZ) and an N-terminally truncated HtrA3S (ΔN-HtrA3S) were fully active at a wide range of temperatures and their substrate affinity was not impaired. This indicates that the PDZ domain is dispensable for HtrA3 activity. As determined by size exclusion chromatography, ΔN-HtrA3 formed stable trimers while both ΔN-HtrA3-ΔPDZ and ΔN-HtrA3S were monomeric. This suggests that the presence of the PDZ domain, unlike in HtrA1 and HtrA2, influences HtrA3 trimer formation. The unique C-terminal sequence of ΔN-HtrA3S appeared to have little effect on activity and oligomerization. Additionally, we examined the cleavage specificity of ΔN-HtrA3. Results reported in this paper provide new insights into the structure and function of ΔN-HtrA3, which seems to have a unique combination of features among human HtrA proteases.},
doi = {10.1371/journal.pone.0131142},
journal = {PLoS ONE},
number = 6,
volume = 10,
place = {United States},
year = {Thu Jun 25 00:00:00 EDT 2015},
month = {Thu Jun 25 00:00:00 EDT 2015}
}
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