Biochemical, molecular genetic, and immunological characterization of a β-1,3-endoglucanase from 'valencia' orange callus
Identifieur interne : 000A26 ( PascalFrancis/Checkpoint ); précédent : 000A25; suivant : 000A27Biochemical, molecular genetic, and immunological characterization of a β-1,3-endoglucanase from 'valencia' orange callus
Auteurs : T. G. Mccollum [États-Unis] ; H. Doostdar [États-Unis] ; R. P. Niedz [États-Unis] ; R. T. Mayer [États-Unis] ; M. Burkhart [États-Unis] ; R. E. Mcdonald [États-Unis]Source :
- Journal of plant physiology [ 0176-1617 ] ; 1999.
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Abstract
We have purified a β-1,3-endoglucanase (EC 3.2.1.39) from nonembryogenic Citrus sinensis (L.) Osbeck cv. Valencia callus to electrophoretic homogeneity by means of pH precipitation and ion exchange chromatography. The protein has an apparent Mr of 32,000, a pI >pH 10 and is serologically similar to a potato leaf glucanase induced by Phytophthora infestans infection. The enzyme hydrolyzes laminarin (Laminaria digitata) optimally at pH 5 and 50°C. The enzyme will hydrolyze pachyman and laminarin extensively and yeast glucan slightly, but does not hydrolyze lichenin, barley glucan, cellulose, or starch. Product characterization by thin-layer chromatography indicates that the enzyme is an endohydrolase. The protein is N-terminal blocked, however, partial internal amino acid sequence analysis revealed that the peptide shared homology with a number of β-1,3-endoglucanases. Antibody to the purified protein was raised in a rabbit and used to screen an amplified cDNA library prepared from Citrus sinensis (L.) Osbeck cv. Valencia callus. A positive clone (pBGVC-1) containing a 1,249 bp insert was isolated. A full length sequence of the clone was obtained and it contained a 1,229 bp open reading frame starting at nucleotide 20. Sequence analysis indicated that the clone is homologous to other β-1,3-endoglucanase genes. The predicted amino acid sequence was homologous with other β-1,3-glucanases, contained both N- and C-terminal signal sequences, the glycosyl hydrolase family 17 signature sequence, and the sequence identical to the peptide that was sequenced from the purified protein.
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G." last="Mccollum">T. G. Mccollum</name><affiliation wicri:level="2"><inist:fA14 i1="01"><s1>USDA, ARS, USHRL, 2120 Camden Rd.</s1><s2>Orlando, FL 32803</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>États-Unis</country><placeName><region type="state">Floride</region></placeName></affiliation></author><author><name sortKey="Doostdar, H" sort="Doostdar, H" uniqKey="Doostdar H" first="H." last="Doostdar">H. Doostdar</name><affiliation wicri:level="2"><inist:fA14 i1="01"><s1>USDA, ARS, USHRL, 2120 Camden Rd.</s1><s2>Orlando, FL 32803</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>États-Unis</country><placeName><region type="state">Floride</region></placeName></affiliation></author><author><name sortKey="Niedz, R P" sort="Niedz, R P" uniqKey="Niedz R" first="R. P." last="Niedz">R. P. 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Burkhart</name><affiliation wicri:level="2"><inist:fA14 i1="01"><s1>USDA, ARS, USHRL, 2120 Camden Rd.</s1><s2>Orlando, FL 32803</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>États-Unis</country><placeName><region type="state">Floride</region></placeName></affiliation></author><author><name sortKey="Mcdonald, R E" sort="Mcdonald, R E" uniqKey="Mcdonald R" first="R. E." last="Mcdonald">R. E. Mcdonald</name><affiliation wicri:level="2"><inist:fA14 i1="01"><s1>USDA, ARS, USHRL, 2120 Camden Rd.</s1><s2>Orlando, FL 32803</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>États-Unis</country><placeName><region type="state">Floride</region></placeName></affiliation></author></analytic><series><title level="j" type="main">Journal of plant physiology</title><title level="j" type="abbreviated">J. plant physiol.</title><idno type="ISSN">0176-1617</idno><imprint><date when="1999">1999</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of plant physiology</title><title level="j" type="abbreviated">J. plant physiol.</title><idno type="ISSN">0176-1617</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aminoacid sequence</term><term>Callus</term><term>Characterization</term><term>Citrus sinensis</term><term>Enzymatic activity</term><term>Glucan-endo-1,3-β-D-glucosidase</term><term>Homology</term><term>Purification</term><term>Substrate specificity</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Glucan-endo-1,3-β-D-glucosidase</term><term>Purification</term><term>Cal</term><term>Caractérisation</term><term>Séquence aminoacide</term><term>Homologie</term><term>Activité enzymatique</term><term>Spécificité substrat</term><term>Citrus sinensis</term><term>Laminarine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have purified a β-1,3-endoglucanase (EC 3.2.1.39) from nonembryogenic Citrus sinensis (L.) Osbeck cv. Valencia callus to electrophoretic homogeneity by means of pH precipitation and ion exchange chromatography. The protein has an apparent M<sub>r</sub> of 32,000, a pI >pH 10 and is serologically similar to a potato leaf glucanase induced by Phytophthora infestans infection. The enzyme hydrolyzes laminarin (Laminaria digitata) optimally at pH 5 and 50°C. The enzyme will hydrolyze pachyman and laminarin extensively and yeast glucan slightly, but does not hydrolyze lichenin, barley glucan, cellulose, or starch. Product characterization by thin-layer chromatography indicates that the enzyme is an endohydrolase. The protein is N-terminal blocked, however, partial internal amino acid sequence analysis revealed that the peptide shared homology with a number of β-1,3-endoglucanases. Antibody to the purified protein was raised in a rabbit and used to screen an amplified cDNA library prepared from Citrus sinensis (L.) Osbeck cv. Valencia callus. A positive clone (pBGVC-1) containing a 1,249 bp insert was isolated. A full length sequence of the clone was obtained and it contained a 1,229 bp open reading frame starting at nucleotide 20. Sequence analysis indicated that the clone is homologous to other β-1,3-endoglucanase genes. The predicted amino acid sequence was homologous with other β-1,3-glucanases, contained both N- and C-terminal signal sequences, the glycosyl hydrolase family 17 signature sequence, and the sequence identical to the peptide that was sequenced from the purified protein.</div></front></TEI><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0176-1617</s0></fA01><fA02 i1="01"><s0>JPPHEY</s0></fA02><fA03 i2="1"><s0>J. plant physiol.</s0></fA03><fA05><s2>155</s2></fA05><fA06><s2>1</s2></fA06><fA08 i1="01" i2="1" l="ENG"><s1>Biochemical, molecular genetic, and immunological characterization of a β-1,3-endoglucanase from 'valencia' orange callus</s1></fA08><fA11 i1="01" i2="1"><s1>MCCOLLUM (T. 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All rights reserved.</s1></fA44><fA45><s0>1 p.1/4</s0></fA45><fA47 i1="01" i2="1"><s0>99-0377112</s0></fA47><fA60><s1>P</s1></fA60><fA61><s0>A</s0></fA61><fA64 i1="01" i2="1"><s0>Journal of plant physiology</s0></fA64><fA66 i1="01"><s0>DEU</s0></fA66><fC01 i1="01" l="ENG"><s0>We have purified a β-1,3-endoglucanase (EC 3.2.1.39) from nonembryogenic Citrus sinensis (L.) Osbeck cv. Valencia callus to electrophoretic homogeneity by means of pH precipitation and ion exchange chromatography. The protein has an apparent M<sub>r</sub> of 32,000, a pI >pH 10 and is serologically similar to a potato leaf glucanase induced by Phytophthora infestans infection. The enzyme hydrolyzes laminarin (Laminaria digitata) optimally at pH 5 and 50°C. The enzyme will hydrolyze pachyman and laminarin extensively and yeast glucan slightly, but does not hydrolyze lichenin, barley glucan, cellulose, or starch. Product characterization by thin-layer chromatography indicates that the enzyme is an endohydrolase. The protein is N-terminal blocked, however, partial internal amino acid sequence analysis revealed that the peptide shared homology with a number of β-1,3-endoglucanases. Antibody to the purified protein was raised in a rabbit and used to screen an amplified cDNA library prepared from Citrus sinensis (L.) Osbeck cv. Valencia callus. A positive clone (pBGVC-1) containing a 1,249 bp insert was isolated. A full length sequence of the clone was obtained and it contained a 1,229 bp open reading frame starting at nucleotide 20. Sequence analysis indicated that the clone is homologous to other β-1,3-endoglucanase genes. The predicted amino acid sequence was homologous with other β-1,3-glucanases, contained both N- and C-terminal signal sequences, the glycosyl hydrolase family 17 signature sequence, and the sequence identical to the peptide that was sequenced from the purified protein.</s0></fC01><fC02 i1="01" i2="X"><s0>002A10E05</s0></fC02><fC02 i1="02" i2="X"><s0>002A02E04</s0></fC02><fC03 i1="01" i2="X" l="FRE"><s0>Glucan-endo-1,3-β-D-glucosidase</s0><s2>FE</s2><s5>01</s5><s6>Glucan-endo-«1,3-β-D»-glucosidase</s6></fC03><fC03 i1="01" i2="X" l="ENG"><s0>Glucan-endo-1,3-β-D-glucosidase</s0><s2>FE</s2><s5>01</s5><s6>Glucan-endo-«1,3-β-D»-glucosidase</s6></fC03><fC03 i1="01" i2="X" l="SPA"><s0>Glucan-endo-1,3-β-D-glucosidase</s0><s2>FE</s2><s5>01</s5><s6>Glucan-endo-«1,3-β-D»-glucosidase</s6></fC03><fC03 i1="02" i2="X" l="FRE"><s0>Purification</s0><s5>02</s5></fC03><fC03 i1="02" i2="X" l="ENG"><s0>Purification</s0><s5>02</s5></fC03><fC03 i1="02" i2="X" l="SPA"><s0>Purificación</s0><s5>02</s5></fC03><fC03 i1="03" i2="X" l="FRE"><s0>Cal</s0><s5>03</s5></fC03><fC03 i1="03" i2="X" l="ENG"><s0>Callus</s0><s5>03</s5></fC03><fC03 i1="03" i2="X" l="SPA"><s0>Callo</s0><s5>03</s5></fC03><fC03 i1="04" i2="X" l="FRE"><s0>Caractérisation</s0><s5>04</s5></fC03><fC03 i1="04" i2="X" l="ENG"><s0>Characterization</s0><s5>04</s5></fC03><fC03 i1="04" i2="X" l="SPA"><s0>Caracterización</s0><s5>04</s5></fC03><fC03 i1="05" i2="X" l="FRE"><s0>Séquence aminoacide</s0><s5>05</s5></fC03><fC03 i1="05" i2="X" l="ENG"><s0>Aminoacid sequence</s0><s5>05</s5></fC03><fC03 i1="05" i2="X" l="SPA"><s0>Secuencia aminoácido</s0><s5>05</s5></fC03><fC03 i1="06" i2="X" l="FRE"><s0>Homologie</s0><s5>06</s5></fC03><fC03 i1="06" i2="X" l="ENG"><s0>Homology</s0><s5>06</s5></fC03><fC03 i1="06" i2="X" l="SPA"><s0>Homología</s0><s5>06</s5></fC03><fC03 i1="07" i2="X" l="FRE"><s0>Activité enzymatique</s0><s5>07</s5></fC03><fC03 i1="07" i2="X" l="ENG"><s0>Enzymatic activity</s0><s5>07</s5></fC03><fC03 i1="07" i2="X" l="SPA"><s0>Actividad enzimática</s0><s5>07</s5></fC03><fC03 i1="08" i2="X" l="FRE"><s0>Spécificité substrat</s0><s5>08</s5></fC03><fC03 i1="08" i2="X" l="ENG"><s0>Substrate specificity</s0><s5>08</s5></fC03><fC03 i1="08" i2="X" l="SPA"><s0>Especificidad sustrato</s0><s5>08</s5></fC03><fC03 i1="09" i2="X" l="FRE"><s0>Citrus sinensis</s0><s2>NS</s2><s5>10</s5></fC03><fC03 i1="09" i2="X" l="ENG"><s0>Citrus sinensis</s0><s2>NS</s2><s5>10</s5></fC03><fC03 i1="09" i2="X" l="SPA"><s0>Citrus sinensis</s0><s2>NS</s2><s5>10</s5></fC03><fC03 i1="10" i2="X" l="FRE"><s0>Laminarine</s0><s2>NK</s2><s4>INC</s4><s5>69</s5></fC03><fC07 i1="01" i2="X" l="FRE"><s0>O-Glycosidases</s0><s2>FE</s2><s6>«O»-Glycosidases</s6></fC07><fC07 i1="01" i2="X" l="ENG"><s0>O-Glycosidases</s0><s2>FE</s2><s6>«O»-Glycosidases</s6></fC07><fC07 i1="01" i2="X" l="SPA"><s0>O-Glycosidases</s0><s2>FE</s2><s6>«O»-Glycosidases</s6></fC07><fC07 i1="02" i2="X" l="FRE"><s0>Glycosidases</s0><s2>FE</s2></fC07><fC07 i1="02" i2="X" l="ENG"><s0>Glycosidases</s0><s2>FE</s2></fC07><fC07 i1="02" i2="X" l="SPA"><s0>Glycosidases</s0><s2>FE</s2></fC07><fC07 i1="03" i2="X" l="FRE"><s0>Hydrolases</s0><s2>FE</s2></fC07><fC07 i1="03" i2="X" l="ENG"><s0>Hydrolases</s0><s2>FE</s2></fC07><fC07 i1="03" i2="X" l="SPA"><s0>Hydrolases</s0><s2>FE</s2></fC07><fC07 i1="04" i2="X" l="FRE"><s0>Enzyme</s0></fC07><fC07 i1="04" i2="X" l="ENG"><s0>Enzyme</s0></fC07><fC07 i1="04" i2="X" l="SPA"><s0>Enzima</s0></fC07><fC07 i1="05" i2="X" l="FRE"><s0>Rutaceae</s0><s2>NS</s2></fC07><fC07 i1="05" i2="X" l="ENG"><s0>Rutaceae</s0><s2>NS</s2></fC07><fC07 i1="05" i2="X" l="SPA"><s0>Rutaceae</s0><s2>NS</s2></fC07><fC07 i1="06" i2="X" l="FRE"><s0>Dicotyledones</s0><s2>NS</s2></fC07><fC07 i1="06" i2="X" l="ENG"><s0>Dicotyledones</s0><s2>NS</s2></fC07><fC07 i1="06" i2="X" l="SPA"><s0>Dicotyledones</s0><s2>NS</s2></fC07><fC07 i1="07" i2="X" l="FRE"><s0>Angiospermae</s0><s2>NS</s2></fC07><fC07 i1="07" i2="X" l="ENG"><s0>Angiospermae</s0><s2>NS</s2></fC07><fC07 i1="07" i2="X" l="SPA"><s0>Angiospermae</s0><s2>NS</s2></fC07><fC07 i1="08" i2="X" l="FRE"><s0>Spermatophyta</s0><s2>NS</s2></fC07><fC07 i1="08" i2="X" l="ENG"><s0>Spermatophyta</s0><s2>NS</s2></fC07><fC07 i1="08" i2="X" l="SPA"><s0>Spermatophyta</s0><s2>NS</s2></fC07><fC07 i1="09" i2="X" l="FRE"><s0>Agrume</s0><s5>40</s5></fC07><fC07 i1="09" i2="X" l="ENG"><s0>Citrus fruit</s0><s5>40</s5></fC07><fC07 i1="09" i2="X" l="SPA"><s0>Agrios</s0><s5>40</s5></fC07><fN21><s1>242</s1></fN21></pA></standard></inist><affiliations><list><country><li>États-Unis</li></country><region><li>Floride</li></region></list><tree><country name="États-Unis"><region name="Floride"><name sortKey="Mccollum, T G" sort="Mccollum, T G" uniqKey="Mccollum T" first="T. G." last="Mccollum">T. G. Mccollum</name></region><name sortKey="Burkhart, M" sort="Burkhart, M" uniqKey="Burkhart M" first="M." last="Burkhart">M. Burkhart</name><name sortKey="Doostdar, H" sort="Doostdar, H" uniqKey="Doostdar H" first="H." last="Doostdar">H. Doostdar</name><name sortKey="Mayer, R T" sort="Mayer, R T" uniqKey="Mayer R" first="R. T." last="Mayer">R. T. Mayer</name><name sortKey="Mcdonald, R E" sort="Mcdonald, R E" uniqKey="Mcdonald R" first="R. E." last="Mcdonald">R. E. Mcdonald</name><name sortKey="Niedz, R P" sort="Niedz, R P" uniqKey="Niedz R" first="R. P." last="Niedz">R. P. Niedz</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Biochemical, molecular genetic, and immunological characterization of a β-1,3-endoglucanase from 'valencia' orange callus
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