Structural and Functional Features of a Wheat Germin-Like Protein that Inhibits Trypsin
The wheat leaf apoplast contains a protein that inhibits trypsin and belongs to the family of germin-like proteins called germin-like protease inhibitor (GLPI). Since it was first described in our laboratory, the objective of this study was to find out if GLPI is a new germin-like protein and to ide...
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| Veröffentlicht in: | Plant molecular biology reporter 2012-06, Vol.30 (3), p.624-632 |
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| creator | Mansilla, Andrea Yamila Segarra, Carmen Inés Conde, Rubén Danilo |
| description | The wheat leaf apoplast contains a protein that inhibits trypsin and belongs to the family of germin-like proteins called germin-like protease inhibitor (GLPI). Since it was first described in our laboratory, the objective of this study was to find out if GLPI is a new germin-like protein and to identify the molecular site responsible for its inhibitory action. Amino acid sequence fragments of GLPI have been determined using mass spectrometry and used to synthesize complementary DNA by reverse transcription PCR. This has allowed recovery of the amino acid sequence of the mature form of GLPI, which is indistinguishable from barley GLP and having pyrophosphatase/phosphodiesterase activity. Using chemical modifiers of amino acids, the unique Arg of GLPI is found to be necessary for preserving its protease inhibition activity. Furthermore, structural homology modeling has allowed prediction that Arg is located along the GLPI surface, which could aid in its activity on proteases. Given that GLPI acts as a superoxide dismutase and as pyrophosphatase/phosphodiesterase, it is deemed to be a multifunctional protein. |
| doi_str_mv | 10.1007/s11105-011-0372-8 |
| format | Article |
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Since it was first described in our laboratory, the objective of this study was to find out if GLPI is a new germin-like protein and to identify the molecular site responsible for its inhibitory action. Amino acid sequence fragments of GLPI have been determined using mass spectrometry and used to synthesize complementary DNA by reverse transcription PCR. This has allowed recovery of the amino acid sequence of the mature form of GLPI, which is indistinguishable from barley GLP and having pyrophosphatase/phosphodiesterase activity. Using chemical modifiers of amino acids, the unique Arg of GLPI is found to be necessary for preserving its protease inhibition activity. Furthermore, structural homology modeling has allowed prediction that Arg is located along the GLPI surface, which could aid in its activity on proteases. 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Since it was first described in our laboratory, the objective of this study was to find out if GLPI is a new germin-like protein and to identify the molecular site responsible for its inhibitory action. Amino acid sequence fragments of GLPI have been determined using mass spectrometry and used to synthesize complementary DNA by reverse transcription PCR. This has allowed recovery of the amino acid sequence of the mature form of GLPI, which is indistinguishable from barley GLP and having pyrophosphatase/phosphodiesterase activity. Using chemical modifiers of amino acids, the unique Arg of GLPI is found to be necessary for preserving its protease inhibition activity. Furthermore, structural homology modeling has allowed prediction that Arg is located along the GLPI surface, which could aid in its activity on proteases. Given that GLPI acts as a superoxide dismutase and as pyrophosphatase/phosphodiesterase, it is deemed to be a multifunctional protein.</description><subject>Amino acid sequence</subject><subject>Amino acids</subject><subject>Apoplast</subject><subject>Barley</subject><subject>Bioinformatics</subject><subject>Biomedical and Life Sciences</subject><subject>Complementary DNA</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Homology</subject><subject>Life Sciences</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Metabolomics</subject><subject>Phosphodiesterase</subject><subject>Plant Breeding/Biotechnology</subject><subject>Plant Sciences</subject><subject>Protease</subject><subject>Proteinase inhibitors</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Pyrophosphatase</subject><subject>Reverse transcription</subject><subject>Structure-function relationships</subject><subject>Superoxide dismutase</subject><subject>Trypsin</subject><subject>Wheat</subject><issn>0735-9640</issn><issn>1572-9818</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kEtLAzEUhYMoWKs_wF3AdfQm02QySyn2AQUFK12GzExiU9tMTTKL_ntTxoUbV_d1zuHyIXRP4ZEClE-RUgqcAKUEipIReYFGlOemklReohGUBSeVmMA1uolxB9kDUo7Q5j2Fvkl90HusfYtnvW-S63weZ0bnvYm4s1jjzTaPeG7CwXmycl8Gv4UuGedx2ubD0m9d7VLE63A6Rudv0ZXV-2jufusYfcxe1tMFWb3Ol9PnFWkKKhJhrJWsZk1VT8DotmpZ09qSV4UoCtty4NpoKwyVVtvailLUVnJeNqIGLmtGizF6GHKPofvuTUxq1_Uhvx8VrbiAUogKsooOqiZ0MQZj1TG4gw4nRUGd-amBn8r81JmfktnDBk_MWv9pwp_kf00_rxpzOA</recordid><startdate>20120601</startdate><enddate>20120601</enddate><creator>Mansilla, Andrea Yamila</creator><creator>Segarra, Carmen Inés</creator><creator>Conde, Rubén Danilo</creator><general>Springer-Verlag</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M0K</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope></search><sort><creationdate>20120601</creationdate><title>Structural and Functional Features of a Wheat Germin-Like Protein that Inhibits Trypsin</title><author>Mansilla, Andrea Yamila ; Segarra, Carmen Inés ; Conde, Rubén Danilo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c316t-22d82b2c9b40ead9d2cdf7593633fd505aeaf6e18fafbf676bf8557c6b058b213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino acid sequence</topic><topic>Amino acids</topic><topic>Apoplast</topic><topic>Barley</topic><topic>Bioinformatics</topic><topic>Biomedical and Life Sciences</topic><topic>Complementary DNA</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>Homology</topic><topic>Life Sciences</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Metabolomics</topic><topic>Phosphodiesterase</topic><topic>Plant Breeding/Biotechnology</topic><topic>Plant Sciences</topic><topic>Protease</topic><topic>Proteinase inhibitors</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>Pyrophosphatase</topic><topic>Reverse transcription</topic><topic>Structure-function relationships</topic><topic>Superoxide dismutase</topic><topic>Trypsin</topic><topic>Wheat</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mansilla, Andrea Yamila</creatorcontrib><creatorcontrib>Segarra, Carmen Inés</creatorcontrib><creatorcontrib>Conde, Rubén Danilo</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><jtitle>Plant molecular biology reporter</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mansilla, Andrea Yamila</au><au>Segarra, Carmen Inés</au><au>Conde, Rubén Danilo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural and Functional Features of a Wheat Germin-Like Protein that Inhibits Trypsin</atitle><jtitle>Plant molecular biology reporter</jtitle><stitle>Plant Mol Biol Rep</stitle><date>2012-06-01</date><risdate>2012</risdate><volume>30</volume><issue>3</issue><spage>624</spage><epage>632</epage><pages>624-632</pages><issn>0735-9640</issn><eissn>1572-9818</eissn><abstract>The wheat leaf apoplast contains a protein that inhibits trypsin and belongs to the family of germin-like proteins called germin-like protease inhibitor (GLPI). Since it was first described in our laboratory, the objective of this study was to find out if GLPI is a new germin-like protein and to identify the molecular site responsible for its inhibitory action. Amino acid sequence fragments of GLPI have been determined using mass spectrometry and used to synthesize complementary DNA by reverse transcription PCR. This has allowed recovery of the amino acid sequence of the mature form of GLPI, which is indistinguishable from barley GLP and having pyrophosphatase/phosphodiesterase activity. Using chemical modifiers of amino acids, the unique Arg of GLPI is found to be necessary for preserving its protease inhibition activity. Furthermore, structural homology modeling has allowed prediction that Arg is located along the GLPI surface, which could aid in its activity on proteases. 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| subjects | Amino acid sequence Amino acids Apoplast Barley Bioinformatics Biomedical and Life Sciences Complementary DNA Deoxyribonucleic acid DNA Homology Life Sciences Mass spectrometry Mass spectroscopy Metabolomics Phosphodiesterase Plant Breeding/Biotechnology Plant Sciences Protease Proteinase inhibitors Proteins Proteomics Pyrophosphatase Reverse transcription Structure-function relationships Superoxide dismutase Trypsin Wheat |
| title | Structural and Functional Features of a Wheat Germin-Like Protein that Inhibits Trypsin |
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