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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Proteolytic activation of <italic>Chlamydia trachomatis</italic>
HTRA is mediated by PDZ1 domain interactions with protease domain loops L3 and LC and beta strand β5</title>
<author><name sortKey="Marsh, James W" sort="Marsh, James W" uniqKey="Marsh J" first="James W." last="Marsh">James W. Marsh</name>
<affiliation><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id>
<institution-id institution-id-type="ISNI">0000000089150953</institution-id>
<institution>Institute of Health and Biomedical Innovation (IHBI),</institution>
<institution>Queensland University of Technology (QUT),</institution>
</institution-wrap>
60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Lott, William B" sort="Lott, William B" uniqKey="Lott W" first="William B." last="Lott">William B. Lott</name>
<affiliation><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id>
<institution-id institution-id-type="ISNI">0000000089150953</institution-id>
<institution>Institute of Health and Biomedical Innovation (IHBI),</institution>
<institution>Queensland University of Technology (QUT),</institution>
</institution-wrap>
60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Tyndall, Joel D A" sort="Tyndall, Joel D A" uniqKey="Tyndall J" first="Joel D. A." last="Tyndall">Joel D. A. Tyndall</name>
<affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="GRID">grid.29980.3a</institution-id>
<institution-id institution-id-type="ISNI">0000000419367830</institution-id>
<institution>National School of Pharmacy,</institution>
<institution>University of Otago,</institution>
</institution-wrap>
PO Box 56, Dunedin, New Zealand 9054</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Huston, Wilhelmina Willa M" sort="Huston, Wilhelmina Willa M" uniqKey="Huston W" first="Wilhelmina Willa M." last="Huston">Wilhelmina Willa M. Huston</name>
<affiliation><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id>
<institution-id institution-id-type="ISNI">0000000089150953</institution-id>
<institution>Institute of Health and Biomedical Innovation (IHBI),</institution>
<institution>Queensland University of Technology (QUT),</institution>
</institution-wrap>
60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</nlm:aff>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">24036669</idno>
<idno type="pmc">6275972</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6275972</idno>
<idno type="RBID">PMC:6275972</idno>
<idno type="doi">10.2478/s11658-013-0103-2</idno>
<date when="2013">2013</date>
<idno type="wicri:Area/Pmc/Corpus">000347</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000347</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Proteolytic activation of <italic>Chlamydia trachomatis</italic>
HTRA is mediated by PDZ1 domain interactions with protease domain loops L3 and LC and beta strand β5</title>
<author><name sortKey="Marsh, James W" sort="Marsh, James W" uniqKey="Marsh J" first="James W." last="Marsh">James W. Marsh</name>
<affiliation><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id>
<institution-id institution-id-type="ISNI">0000000089150953</institution-id>
<institution>Institute of Health and Biomedical Innovation (IHBI),</institution>
<institution>Queensland University of Technology (QUT),</institution>
</institution-wrap>
60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Lott, William B" sort="Lott, William B" uniqKey="Lott W" first="William B." last="Lott">William B. Lott</name>
<affiliation><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id>
<institution-id institution-id-type="ISNI">0000000089150953</institution-id>
<institution>Institute of Health and Biomedical Innovation (IHBI),</institution>
<institution>Queensland University of Technology (QUT),</institution>
</institution-wrap>
60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Tyndall, Joel D A" sort="Tyndall, Joel D A" uniqKey="Tyndall J" first="Joel D. A." last="Tyndall">Joel D. A. Tyndall</name>
<affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="GRID">grid.29980.3a</institution-id>
<institution-id institution-id-type="ISNI">0000000419367830</institution-id>
<institution>National School of Pharmacy,</institution>
<institution>University of Otago,</institution>
</institution-wrap>
PO Box 56, Dunedin, New Zealand 9054</nlm:aff>
</affiliation>
</author>
<author><name sortKey="Huston, Wilhelmina Willa M" sort="Huston, Wilhelmina Willa M" uniqKey="Huston W" first="Wilhelmina Willa M." last="Huston">Wilhelmina Willa M. Huston</name>
<affiliation><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id>
<institution-id institution-id-type="ISNI">0000000089150953</institution-id>
<institution>Institute of Health and Biomedical Innovation (IHBI),</institution>
<institution>Queensland University of Technology (QUT),</institution>
</institution-wrap>
60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</nlm:aff>
</affiliation>
</author>
</analytic>
<series><title level="j">Cellular & Molecular Biology Letters</title>
<idno type="ISSN">1425-8153</idno>
<idno type="eISSN">1689-1392</idno>
<imprint><date when="2013">2013</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p><italic>Chlamydia trachomatis</italic>
is a bacterial pathogen responsible for one of the most prevalent sexually transmitted infections worldwide. Its unique development cycle has limited our understanding of its pathogenic mechanisms. However, CtHtrA has recently been identified as a potential <italic>C. trachomatis</italic>
virulence factor. CtHtrA is a tightly regulated quality control protein with a monomeric structural unit comprised of a chymotrypsin-like protease domain and two PDZ domains. Activation of proteolytic activity relies on the C-terminus of the substrate allosterically binding to the PDZ1 domain, which triggers subsequent conformational change and oligomerization of the protein into 24-mers enabling proteolysis. This activation is mediated by a cascade of precise structural arrangements, but the specific CtHtrA residues and structural elements required to facilitate activation are unknown. Using <italic>in vitro</italic>
analysis guided by homology modeling, we show that the mutation of residues Arg362 and Arg224, predicted to disrupt the interaction between the CtHtrA PDZ1 domain and loop L3, and between loop L3 and loop LD, respectively, are critical for the activation of proteolytic activity. We also demonstrate that mutation to residues Arg299 and Lys160, predicted to disrupt PDZ1 domain interactions with protease loop LC and strand β5, are also able to influence proteolysis, implying their involvement in the CtHtrA mechanism of activation. This is the first investigation of protease loop LC and strand β5 with respect to their potential interactions with the PDZ1 domain. Given their high level of conservation in bacterial HtrA, these structural elements may be equally significant in the activation mechanism of DegP and other HtrA family members.</p>
</div>
</front>
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<front><journal-meta><journal-id journal-id-type="nlm-ta">Cell Mol Biol Lett</journal-id>
<journal-id journal-id-type="iso-abbrev">Cell. Mol. Biol. Lett</journal-id>
<journal-title-group><journal-title>Cellular & Molecular Biology Letters</journal-title>
</journal-title-group>
<issn pub-type="ppub">1425-8153</issn>
<issn pub-type="epub">1689-1392</issn>
<publisher><publisher-name>Springer Vienna</publisher-name>
<publisher-loc>Vienna</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">24036669</article-id>
<article-id pub-id-type="pmc">6275972</article-id>
<article-id pub-id-type="publisher-id">103</article-id>
<article-id pub-id-type="doi">10.2478/s11658-013-0103-2</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Proteolytic activation of <italic>Chlamydia trachomatis</italic>
HTRA is mediated by PDZ1 domain interactions with protease domain loops L3 and LC and beta strand β5</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Marsh</surname>
<given-names>James W.</given-names>
</name>
<xref ref-type="aff" rid="Aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Lott</surname>
<given-names>William B.</given-names>
</name>
<xref ref-type="aff" rid="Aff1">1</xref>
</contrib>
<contrib contrib-type="author" corresp="yes"><name><surname>Tyndall</surname>
<given-names>Joel D. A.</given-names>
</name>
<address><phone>+64 3 4797293</phone>
<fax>+64 3 4797034</fax>
<email>joel.tyndall@otago.ac.nz</email>
</address>
<xref ref-type="aff" rid="Aff2">2</xref>
</contrib>
<contrib contrib-type="author" corresp="yes"><name><surname>Huston</surname>
<given-names>Wilhelmina Willa M.</given-names>
</name>
<address><phone>+61 7 3138 6258</phone>
<fax>+61 7 3138 6030</fax>
<email>w.huston@qut.edu.au</email>
</address>
<xref ref-type="aff" rid="Aff1">1</xref>
</contrib>
<aff id="Aff1"><label>1</label>
<institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id>
<institution-id institution-id-type="ISNI">0000000089150953</institution-id>
<institution>Institute of Health and Biomedical Innovation (IHBI),</institution>
<institution>Queensland University of Technology (QUT),</institution>
</institution-wrap>
60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</aff>
<aff id="Aff2"><label>2</label>
<institution-wrap><institution-id institution-id-type="GRID">grid.29980.3a</institution-id>
<institution-id institution-id-type="ISNI">0000000419367830</institution-id>
<institution>National School of Pharmacy,</institution>
<institution>University of Otago,</institution>
</institution-wrap>
PO Box 56, Dunedin, New Zealand 9054</aff>
</contrib-group>
<pub-date pub-type="epub"><day>13</day>
<month>9</month>
<year>2013</year>
</pub-date>
<pub-date pub-type="collection"><month>12</month>
<year>2013</year>
</pub-date>
<volume>18</volume>
<issue>4</issue>
<fpage>522</fpage>
<lpage>537</lpage>
<history><date date-type="received"><day>14</day>
<month>6</month>
<year>2013</year>
</date>
<date date-type="accepted"><day>9</day>
<month>9</month>
<year>2013</year>
</date>
</history>
<permissions><copyright-statement>© Versita Warsaw and Springer-Verlag Wien 2013</copyright-statement>
</permissions>
<abstract id="Abs1"><p><italic>Chlamydia trachomatis</italic>
is a bacterial pathogen responsible for one of the most prevalent sexually transmitted infections worldwide. Its unique development cycle has limited our understanding of its pathogenic mechanisms. However, CtHtrA has recently been identified as a potential <italic>C. trachomatis</italic>
virulence factor. CtHtrA is a tightly regulated quality control protein with a monomeric structural unit comprised of a chymotrypsin-like protease domain and two PDZ domains. Activation of proteolytic activity relies on the C-terminus of the substrate allosterically binding to the PDZ1 domain, which triggers subsequent conformational change and oligomerization of the protein into 24-mers enabling proteolysis. This activation is mediated by a cascade of precise structural arrangements, but the specific CtHtrA residues and structural elements required to facilitate activation are unknown. Using <italic>in vitro</italic>
analysis guided by homology modeling, we show that the mutation of residues Arg362 and Arg224, predicted to disrupt the interaction between the CtHtrA PDZ1 domain and loop L3, and between loop L3 and loop LD, respectively, are critical for the activation of proteolytic activity. We also demonstrate that mutation to residues Arg299 and Lys160, predicted to disrupt PDZ1 domain interactions with protease loop LC and strand β5, are also able to influence proteolysis, implying their involvement in the CtHtrA mechanism of activation. This is the first investigation of protease loop LC and strand β5 with respect to their potential interactions with the PDZ1 domain. Given their high level of conservation in bacterial HtrA, these structural elements may be equally significant in the activation mechanism of DegP and other HtrA family members.</p>
</abstract>
<kwd-group xml:lang="en"><title>Key words</title>
<kwd><italic>Chlamydia</italic>
</kwd>
<kwd>HtrA</kwd>
<kwd>DegP</kwd>
<kwd>Protease</kwd>
<kwd>Oligomerization</kwd>
</kwd-group>
<custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name>
<meta-value>© Versita Warsaw and Springer-Verlag Wien 2013</meta-value>
</custom-meta>
</custom-meta-group>
</article-meta>
</front>
<back><glossary><title>Abbreviations used</title>
<def-list><def-item><term>CD</term>
<def><p>circular dichroism</p>
</def>
</def-item>
<def-item><term>CtHtrA</term>
<def><p><italic>Chlamydia trachomatis</italic>
high temperature requirement A</p>
</def>
</def-item>
<def-item><term>MCA</term>
<def><p>7-methoxycoumarin-4-acetic acid</p>
</def>
</def-item>
<def-item><term>MOMP</term>
<def><p>major outer membrane protein</p>
</def>
</def-item>
<def-item><term>MRW</term>
<def><p>mean residue weight</p>
</def>
</def-item>
<def-item><term>OmpA</term>
<def><p>outer membrane protein A</p>
</def>
</def-item>
<def-item><term>PDZ</term>
<def><p>PSD-95/Dics-Large/ZO-1</p>
</def>
</def-item>
<def-item><term>PmpC</term>
<def><p>polymorphic membrane protein C</p>
</def>
</def-item>
<def-item><term>pNA</term>
<def><p><italic>para</italic>
-nitroalinine</p>
</def>
</def-item>
<def-item><term>SDM</term>
<def><p>site-directed mutagenesis</p>
</def>
</def-item>
<def-item><term>SDS-PAGE</term>
<def><p>sodium dodecyl sulphate polyacrylamide gel electrophoresis</p>
</def>
</def-item>
</def-list>
</glossary>
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