Characterization of a novel otubain-like cysteine protease of Cryptosporidium parvum
Abstract Otubains are a recently discovered family of cysteine proteases that participate in the ubiquitin pathway. Here, we partially characterized the biochemical properties of a cysteine protease of Cryptosporidium parvum , which is closely related to otubains. The gene encoding otubain-like cyst...
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| Veröffentlicht in: | Parasitology international 2014-08, Vol.63 (4), p.580-583 |
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| creator | Ju, Hye-Lim Kang, Jung-Mi Noh, Hae Sook Kim, Deok Ryong Hong, Yeonchul Sohn, Woon-Mok Na, Byoung-Kuk |
| description | Abstract Otubains are a recently discovered family of cysteine proteases that participate in the ubiquitin pathway. Here, we partially characterized the biochemical properties of a cysteine protease of Cryptosporidium parvum , which is closely related to otubains. The gene encoding otubain-like cysteine protease of C. parvum (CpOTU) contained the aspartate, cysteine and histidine residues that form the catalytic triad of otubains. The modified ubiquitin-associated domain and LxxL motif were identified in CpOTU. The recombinant CpOTU showed the isopeptidase activity at neutral pH values and its activity was effectively inhibited by ubiquitin aldehyde, N-ethylmaleimide and iodoacetic acid. Interestingly, CpOTU had an unusual C-terminal extension of 217 amino acids compared to mammalian otubains, and the C-terminal extension is essential for the activity of the enzyme. Expression of CpOTU peaked in the oocyst stage of the parasite, which suggested its potential physiological role for the oocyst stage. |
| doi_str_mv | 10.1016/j.parint.2014.03.005 |
| format | Article |
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Here, we partially characterized the biochemical properties of a cysteine protease of Cryptosporidium parvum , which is closely related to otubains. The gene encoding otubain-like cysteine protease of C. parvum (CpOTU) contained the aspartate, cysteine and histidine residues that form the catalytic triad of otubains. The modified ubiquitin-associated domain and LxxL motif were identified in CpOTU. The recombinant CpOTU showed the isopeptidase activity at neutral pH values and its activity was effectively inhibited by ubiquitin aldehyde, N-ethylmaleimide and iodoacetic acid. Interestingly, CpOTU had an unusual C-terminal extension of 217 amino acids compared to mammalian otubains, and the C-terminal extension is essential for the activity of the enzyme. Expression of CpOTU peaked in the oocyst stage of the parasite, which suggested its potential physiological role for the oocyst stage.</description><identifier>ISSN: 1383-5769</identifier><identifier>EISSN: 1873-0329</identifier><identifier>DOI: 10.1016/j.parint.2014.03.005</identifier><identifier>PMID: 24709083</identifier><language>eng</language><publisher>Netherlands: Elsevier Ireland Ltd</publisher><subject>Amino Acid Sequence ; Cryptosporidium parvum ; Cryptosporidium parvum - enzymology ; Cryptosporidium parvum - genetics ; Cryptosporidium parvum - metabolism ; Cysteine protease ; Cysteine Proteases - chemistry ; Cysteine Proteases - genetics ; Cysteine Proteases - metabolism ; Gastroenterology and Hepatology ; Infectious Disease ; Molecular Sequence Data ; Oocyst ; Otubain ; Protein Structure, Tertiary ; Protozoan Proteins - chemistry ; Protozoan Proteins - genetics ; Protozoan Proteins - metabolism ; Ubiquitin pathway</subject><ispartof>Parasitology international, 2014-08, Vol.63 (4), p.580-583</ispartof><rights>Elsevier Ireland Ltd</rights><rights>2014 Elsevier Ireland Ltd</rights><rights>Copyright © 2014 Elsevier Ireland Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-63f917a067c19fb60b0d06bc07eda8ad443627ab3479e7873ee39aa3c9a2d7c23</citedby><cites>FETCH-LOGICAL-c474t-63f917a067c19fb60b0d06bc07eda8ad443627ab3479e7873ee39aa3c9a2d7c23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1383576914000361$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24709083$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ju, Hye-Lim</creatorcontrib><creatorcontrib>Kang, Jung-Mi</creatorcontrib><creatorcontrib>Noh, Hae Sook</creatorcontrib><creatorcontrib>Kim, Deok Ryong</creatorcontrib><creatorcontrib>Hong, Yeonchul</creatorcontrib><creatorcontrib>Sohn, Woon-Mok</creatorcontrib><creatorcontrib>Na, Byoung-Kuk</creatorcontrib><title>Characterization of a novel otubain-like cysteine protease of Cryptosporidium parvum</title><title>Parasitology international</title><addtitle>Parasitol Int</addtitle><description>Abstract Otubains are a recently discovered family of cysteine proteases that participate in the ubiquitin pathway. Here, we partially characterized the biochemical properties of a cysteine protease of Cryptosporidium parvum , which is closely related to otubains. The gene encoding otubain-like cysteine protease of C. parvum (CpOTU) contained the aspartate, cysteine and histidine residues that form the catalytic triad of otubains. The modified ubiquitin-associated domain and LxxL motif were identified in CpOTU. The recombinant CpOTU showed the isopeptidase activity at neutral pH values and its activity was effectively inhibited by ubiquitin aldehyde, N-ethylmaleimide and iodoacetic acid. Interestingly, CpOTU had an unusual C-terminal extension of 217 amino acids compared to mammalian otubains, and the C-terminal extension is essential for the activity of the enzyme. Expression of CpOTU peaked in the oocyst stage of the parasite, which suggested its potential physiological role for the oocyst stage.</description><subject>Amino Acid Sequence</subject><subject>Cryptosporidium parvum</subject><subject>Cryptosporidium parvum - enzymology</subject><subject>Cryptosporidium parvum - genetics</subject><subject>Cryptosporidium parvum - metabolism</subject><subject>Cysteine protease</subject><subject>Cysteine Proteases - chemistry</subject><subject>Cysteine Proteases - genetics</subject><subject>Cysteine Proteases - metabolism</subject><subject>Gastroenterology and Hepatology</subject><subject>Infectious Disease</subject><subject>Molecular Sequence Data</subject><subject>Oocyst</subject><subject>Otubain</subject><subject>Protein Structure, Tertiary</subject><subject>Protozoan Proteins - chemistry</subject><subject>Protozoan Proteins - genetics</subject><subject>Protozoan Proteins - metabolism</subject><subject>Ubiquitin pathway</subject><issn>1383-5769</issn><issn>1873-0329</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUtv1DAQgCNERUvLP0AoRy4J49iJ1xcktOIlVeLQ9mxNnInwNrGD7ay0_HocbeHABU4zh29e3xTFawY1A9a9O9QLButS3QATNfAaoH1WXLGd5BXwRj3POd_xqpWduixexngAYK2U7EVx2QgJCnb8qrjff8eAJlGwPzFZ70o_llg6f6Sp9Gnt0bpqso9UmlNMZB2VS_CJMNJG7sNpST4uPtjBrnOZVzqu801xMeIU6dVTvC4ePn2833-pbr99_rr_cFsZIUWqOj4qJhE6aZga-w56GKDrDUgacIeDELxrJPZcSEUy30XEFSI3CptBmoZfF2_PffNKP1aKSc82GpomdOTXqFkrBDCp2vY_UA6qbVolMirOqAk-xkCjXoKdMZw0A72p1wd9Vq839Rq4zupz2ZunCWs_0_Cn6LfrDLw_A5SVHC0FHY0lZ2iwgUzSg7f_mvB3AzNZZw1Oj3SiePBrcFm3Zjo2GvTd9v7t-0wAAO8Y_wUALqxg</recordid><startdate>20140801</startdate><enddate>20140801</enddate><creator>Ju, Hye-Lim</creator><creator>Kang, Jung-Mi</creator><creator>Noh, Hae Sook</creator><creator>Kim, Deok Ryong</creator><creator>Hong, Yeonchul</creator><creator>Sohn, Woon-Mok</creator><creator>Na, Byoung-Kuk</creator><general>Elsevier Ireland Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>M7N</scope></search><sort><creationdate>20140801</creationdate><title>Characterization of a novel otubain-like cysteine protease of Cryptosporidium parvum</title><author>Ju, Hye-Lim ; Kang, Jung-Mi ; Noh, Hae Sook ; Kim, Deok Ryong ; Hong, Yeonchul ; Sohn, Woon-Mok ; Na, Byoung-Kuk</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-63f917a067c19fb60b0d06bc07eda8ad443627ab3479e7873ee39aa3c9a2d7c23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>Cryptosporidium parvum</topic><topic>Cryptosporidium parvum - enzymology</topic><topic>Cryptosporidium parvum - genetics</topic><topic>Cryptosporidium parvum - metabolism</topic><topic>Cysteine protease</topic><topic>Cysteine Proteases - chemistry</topic><topic>Cysteine Proteases - genetics</topic><topic>Cysteine Proteases - metabolism</topic><topic>Gastroenterology and Hepatology</topic><topic>Infectious Disease</topic><topic>Molecular Sequence Data</topic><topic>Oocyst</topic><topic>Otubain</topic><topic>Protein Structure, Tertiary</topic><topic>Protozoan Proteins - chemistry</topic><topic>Protozoan Proteins - genetics</topic><topic>Protozoan Proteins - metabolism</topic><topic>Ubiquitin pathway</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ju, Hye-Lim</creatorcontrib><creatorcontrib>Kang, Jung-Mi</creatorcontrib><creatorcontrib>Noh, Hae Sook</creatorcontrib><creatorcontrib>Kim, Deok Ryong</creatorcontrib><creatorcontrib>Hong, Yeonchul</creatorcontrib><creatorcontrib>Sohn, Woon-Mok</creatorcontrib><creatorcontrib>Na, Byoung-Kuk</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Parasitology international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ju, Hye-Lim</au><au>Kang, Jung-Mi</au><au>Noh, Hae Sook</au><au>Kim, Deok Ryong</au><au>Hong, Yeonchul</au><au>Sohn, Woon-Mok</au><au>Na, Byoung-Kuk</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a novel otubain-like cysteine protease of Cryptosporidium parvum</atitle><jtitle>Parasitology international</jtitle><addtitle>Parasitol Int</addtitle><date>2014-08-01</date><risdate>2014</risdate><volume>63</volume><issue>4</issue><spage>580</spage><epage>583</epage><pages>580-583</pages><issn>1383-5769</issn><eissn>1873-0329</eissn><abstract>Abstract Otubains are a recently discovered family of cysteine proteases that participate in the ubiquitin pathway. Here, we partially characterized the biochemical properties of a cysteine protease of Cryptosporidium parvum , which is closely related to otubains. The gene encoding otubain-like cysteine protease of C. parvum (CpOTU) contained the aspartate, cysteine and histidine residues that form the catalytic triad of otubains. The modified ubiquitin-associated domain and LxxL motif were identified in CpOTU. The recombinant CpOTU showed the isopeptidase activity at neutral pH values and its activity was effectively inhibited by ubiquitin aldehyde, N-ethylmaleimide and iodoacetic acid. Interestingly, CpOTU had an unusual C-terminal extension of 217 amino acids compared to mammalian otubains, and the C-terminal extension is essential for the activity of the enzyme. Expression of CpOTU peaked in the oocyst stage of the parasite, which suggested its potential physiological role for the oocyst stage.</abstract><cop>Netherlands</cop><pub>Elsevier Ireland Ltd</pub><pmid>24709083</pmid><doi>10.1016/j.parint.2014.03.005</doi><tpages>4</tpages></addata></record> |
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| subjects | Amino Acid Sequence Cryptosporidium parvum Cryptosporidium parvum - enzymology Cryptosporidium parvum - genetics Cryptosporidium parvum - metabolism Cysteine protease Cysteine Proteases - chemistry Cysteine Proteases - genetics Cysteine Proteases - metabolism Gastroenterology and Hepatology Infectious Disease Molecular Sequence Data Oocyst Otubain Protein Structure, Tertiary Protozoan Proteins - chemistry Protozoan Proteins - genetics Protozoan Proteins - metabolism Ubiquitin pathway |
| title | Characterization of a novel otubain-like cysteine protease of Cryptosporidium parvum |
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