The rust transferred proteins-a new family of effector proteins exhibiting protease inhibitor function
Summary Only few fungal effectors have been described to be delivered into the host cell during obligate biotrophic interactions. RTP1p, from the rust fungi Uromyces fabae and U. striatus, was the first fungal protein for which localization within the host cytoplasm could be demonstrated directly. W...
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| Veröffentlicht in: | Molecular plant pathology 2013-01, Vol.14 (1), p.96-107 |
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| creator | Pretsch, Klara Kemen, Ariane Kemen, Eric Geiger, Matthias Mendgen, Kurt Voegele, Ralf |
| description | Summary
Only few fungal effectors have been described to be delivered into the host cell during obligate biotrophic interactions. RTP1p, from the rust fungi Uromyces fabae and U. striatus, was the first fungal protein for which localization within the host cytoplasm could be demonstrated directly. We investigated the occurrence of RTP1 homologues in rust fungi and examined the structural and biochemical characteristics of the corresponding gene products. The analysis of 28 homologues showed that members of the RTP family are most likely to occur ubiquitously in rust fungi and to be specific to the order Pucciniales. Sequence analyses indicated that the structure of the RTPp effectors is bipartite, consisting of a variable N‐terminus and a conserved and structured C‐terminus. The characterization of Uf‐RTP1p mutants showed that four conserved cysteine residues sustain structural stability. Furthermore, the C‐terminal domain exhibits similarities to that of cysteine protease inhibitors, and it was shown that Uf‐RTP1p and Us‐RTP1p are able to inhibit proteolytic activity in Pichia pastoris culture supernatants. We conclude that the RTP1p homologues constitute a rust fungi‐specific family of modular effector proteins comprising an unstructured N‐terminal domain and a structured C‐terminal domain, which exhibit protease inhibitory activity possibly associated with effector function during biotrophic interactions. |
| doi_str_mv | 10.1111/j.1364-3703.2012.00832.x |
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Only few fungal effectors have been described to be delivered into the host cell during obligate biotrophic interactions. RTP1p, from the rust fungi Uromyces fabae and U. striatus, was the first fungal protein for which localization within the host cytoplasm could be demonstrated directly. We investigated the occurrence of RTP1 homologues in rust fungi and examined the structural and biochemical characteristics of the corresponding gene products. The analysis of 28 homologues showed that members of the RTP family are most likely to occur ubiquitously in rust fungi and to be specific to the order Pucciniales. Sequence analyses indicated that the structure of the RTPp effectors is bipartite, consisting of a variable N‐terminus and a conserved and structured C‐terminus. The characterization of Uf‐RTP1p mutants showed that four conserved cysteine residues sustain structural stability. Furthermore, the C‐terminal domain exhibits similarities to that of cysteine protease inhibitors, and it was shown that Uf‐RTP1p and Us‐RTP1p are able to inhibit proteolytic activity in Pichia pastoris culture supernatants. We conclude that the RTP1p homologues constitute a rust fungi‐specific family of modular effector proteins comprising an unstructured N‐terminal domain and a structured C‐terminal domain, which exhibit protease inhibitory activity possibly associated with effector function during biotrophic interactions.</description><identifier>ISSN: 1464-6722</identifier><identifier>EISSN: 1364-3703</identifier><identifier>DOI: 10.1111/j.1364-3703.2012.00832.x</identifier><identifier>PMID: 22998218</identifier><identifier>CODEN: MPPAFD</identifier><language>eng</language><publisher>Oxford: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Bacteriology ; Basidiomycota - drug effects ; Basidiomycota - metabolism ; Biochemical characteristics ; Biological and medical sciences ; Cysteine Proteinase Inhibitors - chemistry ; Cysteine Proteinase Inhibitors - pharmacology ; Disulfides - metabolism ; Enzymes ; Exons - genetics ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - chemistry ; Fungal Proteins - metabolism ; Fungal Proteins - pharmacology ; Introns - genetics ; Molecular Sequence Data ; Original ; Phylogeny ; Phytopathology. Animal pests. Plant and forest protection ; Pichia - drug effects ; Pichia - metabolism ; Pichia pastoris ; Protease Inhibitors - chemistry ; Protease Inhibitors - metabolism ; Protease Inhibitors - pharmacology ; Protein Stability - drug effects ; Protein Structure, Tertiary ; Proteins ; Proteolysis - drug effects ; Sequence Alignment ; Sequence Homology, Amino Acid</subject><ispartof>Molecular plant pathology, 2013-01, Vol.14 (1), p.96-107</ispartof><rights>2012 THE AUTHORS. MOLECULAR PLANT PATHOLOGY © 2012 BSPP AND BLACKWELL PUBLISHING LTD</rights><rights>2014 INIST-CNRS</rights><rights>2012 THE AUTHORS. MOLECULAR PLANT PATHOLOGY © 2012 BSPP AND BLACKWELL PUBLISHING LTD.</rights><rights>Molecular Plant Pathology © 2012 BSPP and Blackwell Publishing Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6022-a972c6c907aac22af69850941363b8c8161e1fb37722a513a8af68f9ee7f751e3</citedby><cites>FETCH-LOGICAL-c6022-a972c6c907aac22af69850941363b8c8161e1fb37722a513a8af68f9ee7f751e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6638633/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6638633/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,11541,27901,27902,45550,45551,46027,46451,53766,53768</link.rule.ids><linktorsrc>$$Uhttps://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1364-3703.2012.00832.x$$EView_record_in_Wiley-Blackwell$$FView_record_in_$$GWiley-Blackwell</linktorsrc><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26691635$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22998218$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pretsch, Klara</creatorcontrib><creatorcontrib>Kemen, Ariane</creatorcontrib><creatorcontrib>Kemen, Eric</creatorcontrib><creatorcontrib>Geiger, Matthias</creatorcontrib><creatorcontrib>Mendgen, Kurt</creatorcontrib><creatorcontrib>Voegele, Ralf</creatorcontrib><title>The rust transferred proteins-a new family of effector proteins exhibiting protease inhibitor function</title><title>Molecular plant pathology</title><addtitle>Molecular Plant Pathology</addtitle><description>Summary
Only few fungal effectors have been described to be delivered into the host cell during obligate biotrophic interactions. RTP1p, from the rust fungi Uromyces fabae and U. striatus, was the first fungal protein for which localization within the host cytoplasm could be demonstrated directly. We investigated the occurrence of RTP1 homologues in rust fungi and examined the structural and biochemical characteristics of the corresponding gene products. The analysis of 28 homologues showed that members of the RTP family are most likely to occur ubiquitously in rust fungi and to be specific to the order Pucciniales. Sequence analyses indicated that the structure of the RTPp effectors is bipartite, consisting of a variable N‐terminus and a conserved and structured C‐terminus. The characterization of Uf‐RTP1p mutants showed that four conserved cysteine residues sustain structural stability. Furthermore, the C‐terminal domain exhibits similarities to that of cysteine protease inhibitors, and it was shown that Uf‐RTP1p and Us‐RTP1p are able to inhibit proteolytic activity in Pichia pastoris culture supernatants. We conclude that the RTP1p homologues constitute a rust fungi‐specific family of modular effector proteins comprising an unstructured N‐terminal domain and a structured C‐terminal domain, which exhibit protease inhibitory activity possibly associated with effector function during biotrophic interactions.</description><subject>Amino Acid Sequence</subject><subject>Bacteriology</subject><subject>Basidiomycota - drug effects</subject><subject>Basidiomycota - metabolism</subject><subject>Biochemical characteristics</subject><subject>Biological and medical sciences</subject><subject>Cysteine Proteinase Inhibitors - chemistry</subject><subject>Cysteine Proteinase Inhibitors - pharmacology</subject><subject>Disulfides - metabolism</subject><subject>Enzymes</subject><subject>Exons - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - metabolism</subject><subject>Fungal Proteins - pharmacology</subject><subject>Introns - genetics</subject><subject>Molecular Sequence Data</subject><subject>Original</subject><subject>Phylogeny</subject><subject>Phytopathology. Animal pests. Plant and forest protection</subject><subject>Pichia - drug effects</subject><subject>Pichia - metabolism</subject><subject>Pichia pastoris</subject><subject>Protease Inhibitors - chemistry</subject><subject>Protease Inhibitors - metabolism</subject><subject>Protease Inhibitors - pharmacology</subject><subject>Protein Stability - drug effects</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Proteolysis - drug effects</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><issn>1464-6722</issn><issn>1364-3703</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkVtv1DAQhSMEohf4C8gSQuIlwZeNLxJCQiu6RSrQh1IeLa877nrJOls7obv_HqdZwuUJv3g0_s5ojk9RIIIrks-bdUUYn5VMYFZRTGiFsWS02j0qjqeHx7me5ZoLSo-Kk5TWGBOhaP20OKJUKUmJPC7c1QpQ7FOHumhCchAj3KBtbDvwIZUGBbhHzmx8s0etQ-Ac2K6NE4Fgt_JL3_lwO_ZMAuTDQy9jrg-28214Vjxxpknw_HCfFl_PPlzNz8uLL4uP8_cXpeWY0tIoQS23CgtjLKXGcSVrrGbZFFtKKwknQNySiezJ1IQZmRHpFIBwoibATot349xtv9zAjYWQbTV6G_3GxL1ujdd_vwS_0rftD805k5yxPOD1YUBs73pInd74ZKFpTIC2T3r40poQQWhGX_6Drts-hmxPE0oJU4oykik5Uja2KUVw0zIE6yFMvdZDZnrITA9h6ocw9S5LX_xpZhL-Si8Drw6ASdY0LidoffrNca4IZ3Xm3o7cvW9g_98L6E-Xl7nI8nKU-9TBbpKb-F1zwUStv31e6Gsl5tfnC6IZ-wmaD8r_</recordid><startdate>201301</startdate><enddate>201301</enddate><creator>Pretsch, Klara</creator><creator>Kemen, Ariane</creator><creator>Kemen, Eric</creator><creator>Geiger, Matthias</creator><creator>Mendgen, Kurt</creator><creator>Voegele, Ralf</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>John Wiley & Sons, Inc</general><general>John Wiley and Sons Inc</general><scope>BSCLL</scope><scope>IQODW</scope><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>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>5PM</scope></search><sort><creationdate>201301</creationdate><title>The rust transferred proteins-a new family of effector proteins exhibiting protease inhibitor function</title><author>Pretsch, Klara ; Kemen, Ariane ; Kemen, Eric ; Geiger, Matthias ; Mendgen, Kurt ; Voegele, Ralf</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6022-a972c6c907aac22af69850941363b8c8161e1fb37722a513a8af68f9ee7f751e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Sequence</topic><topic>Bacteriology</topic><topic>Basidiomycota - drug effects</topic><topic>Basidiomycota - metabolism</topic><topic>Biochemical characteristics</topic><topic>Biological and medical sciences</topic><topic>Cysteine Proteinase Inhibitors - chemistry</topic><topic>Cysteine Proteinase Inhibitors - pharmacology</topic><topic>Disulfides - metabolism</topic><topic>Enzymes</topic><topic>Exons - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - metabolism</topic><topic>Fungal Proteins - pharmacology</topic><topic>Introns - genetics</topic><topic>Molecular Sequence Data</topic><topic>Original</topic><topic>Phylogeny</topic><topic>Phytopathology. Animal pests. Plant and forest protection</topic><topic>Pichia - drug effects</topic><topic>Pichia - metabolism</topic><topic>Pichia pastoris</topic><topic>Protease Inhibitors - chemistry</topic><topic>Protease Inhibitors - metabolism</topic><topic>Protease Inhibitors - pharmacology</topic><topic>Protein Stability - drug effects</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Proteolysis - drug effects</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pretsch, Klara</creatorcontrib><creatorcontrib>Kemen, Ariane</creatorcontrib><creatorcontrib>Kemen, Eric</creatorcontrib><creatorcontrib>Geiger, Matthias</creatorcontrib><creatorcontrib>Mendgen, Kurt</creatorcontrib><creatorcontrib>Voegele, Ralf</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular plant pathology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Pretsch, Klara</au><au>Kemen, Ariane</au><au>Kemen, Eric</au><au>Geiger, Matthias</au><au>Mendgen, Kurt</au><au>Voegele, Ralf</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The rust transferred proteins-a new family of effector proteins exhibiting protease inhibitor function</atitle><jtitle>Molecular plant pathology</jtitle><addtitle>Molecular Plant Pathology</addtitle><date>2013-01</date><risdate>2013</risdate><volume>14</volume><issue>1</issue><spage>96</spage><epage>107</epage><pages>96-107</pages><issn>1464-6722</issn><eissn>1364-3703</eissn><coden>MPPAFD</coden><abstract>Summary
Only few fungal effectors have been described to be delivered into the host cell during obligate biotrophic interactions. RTP1p, from the rust fungi Uromyces fabae and U. striatus, was the first fungal protein for which localization within the host cytoplasm could be demonstrated directly. We investigated the occurrence of RTP1 homologues in rust fungi and examined the structural and biochemical characteristics of the corresponding gene products. The analysis of 28 homologues showed that members of the RTP family are most likely to occur ubiquitously in rust fungi and to be specific to the order Pucciniales. Sequence analyses indicated that the structure of the RTPp effectors is bipartite, consisting of a variable N‐terminus and a conserved and structured C‐terminus. The characterization of Uf‐RTP1p mutants showed that four conserved cysteine residues sustain structural stability. Furthermore, the C‐terminal domain exhibits similarities to that of cysteine protease inhibitors, and it was shown that Uf‐RTP1p and Us‐RTP1p are able to inhibit proteolytic activity in Pichia pastoris culture supernatants. We conclude that the RTP1p homologues constitute a rust fungi‐specific family of modular effector proteins comprising an unstructured N‐terminal domain and a structured C‐terminal domain, which exhibit protease inhibitory activity possibly associated with effector function during biotrophic interactions.</abstract><cop>Oxford</cop><pub>Blackwell Publishing Ltd</pub><pmid>22998218</pmid><doi>10.1111/j.1364-3703.2012.00832.x</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Bacteriology Basidiomycota - drug effects Basidiomycota - metabolism Biochemical characteristics Biological and medical sciences Cysteine Proteinase Inhibitors - chemistry Cysteine Proteinase Inhibitors - pharmacology Disulfides - metabolism Enzymes Exons - genetics Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Fungal Proteins - metabolism Fungal Proteins - pharmacology Introns - genetics Molecular Sequence Data Original Phylogeny Phytopathology. Animal pests. Plant and forest protection Pichia - drug effects Pichia - metabolism Pichia pastoris Protease Inhibitors - chemistry Protease Inhibitors - metabolism Protease Inhibitors - pharmacology Protein Stability - drug effects Protein Structure, Tertiary Proteins Proteolysis - drug effects Sequence Alignment Sequence Homology, Amino Acid |
| title | The rust transferred proteins-a new family of effector proteins exhibiting protease inhibitor function |
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