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Score: 6.00 |
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| Title: In vivo and in vitro phosphorylation of rice dwarf phytoreovirus Pns12 cytoplasmic nonstructural protein .
| | Author: Suzuki N Hosokawa D Matsuura Y Kikuchi A Omura T | | Journal: Arch . Virol . Citation: V : 144 ( 7 ) P : 1371-80 Year: Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10481743 Accession (PMID): 10481743 | Matching Sentences:
[ Sen. 1, subscore: 1.00 ]: In vivo and in vitro phosphorylation and intracellular location of rice dwarf phytoreovirus Pns12 , which is encoded by one of the twelve dsRNA genome segments , S12 , and comprises 312 amino acids , was investigated . When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody . Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 . Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well . Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch . These results demonstrated that RDV Pns12 was a cytoplasmic nonstructural phosphoprotein .
[ Sen. 2, subscore: 1.00 ]: In vivo and in vitro phosphorylation and intracellular location of rice dwarf phytoreovirus Pns12 , which is encoded by one of the twelve dsRNA genome segments , S12 , and comprises 312 amino acids , was investigated . When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody . Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 . Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well . Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch . These results demonstrated that RDV Pns12 was a cytoplasmic nonstructural phosphoprotein .
[ Sen. 3, subscore: 1.00 ]: In vivo and in vitro phosphorylation and intracellular location of rice dwarf phytoreovirus Pns12 , which is encoded by one of the twelve dsRNA genome segments , S12 , and comprises 312 amino acids , was investigated . When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody . Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 . Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well . Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch . These results demonstrated that RDV Pns12 was a cytoplasmic nonstructural phosphoprotein .
[ Sen. 4, subscore: 1.00 ]: In vivo and in vitro phosphorylation and intracellular location of rice dwarf phytoreovirus Pns12 , which is encoded by one of the twelve dsRNA genome segments , S12 , and comprises 312 amino acids , was investigated . When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody . Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 . Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well . Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch . These results demonstrated that RDV Pns12 was a cytoplasmic nonstructural phosphoprotein .
[ Sen. 5, subscore: 1.00 ]: In vivo and in vitro phosphorylation and intracellular location of rice dwarf phytoreovirus Pns12 , which is encoded by one of the twelve dsRNA genome segments , S12 , and comprises 312 amino acids , was investigated . When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody . Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 . Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well . Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch . These results demonstrated that RDV Pns12 was a cytoplasmic nonstructural phosphoprotein .
[ Sen. 6, subscore: 1.00 ]: In vivo and in vitro phosphorylation and intracellular location of rice dwarf phytoreovirus Pns12 , which is encoded by one of the twelve dsRNA genome segments , S12 , and comprises 312 amino acids , was investigated . When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody . Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 . Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well . Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch . These results demonstrated that RDV Pns12 was a cytoplasmic nonstructural phosphoprotein .
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Score: 3.00 |
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| Title: Glutelin basic subunits have a mammalian mucin-type O-linked disaccharide side chain .
| | Author: Kishimoto T Watanabe M Mitsui T Hori H | | Journal: Arch . Biochem . Biophys . Citation: V : 370 ( 2 ) P : 271-7 Year: 1999 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10510286 Accession (PMID): 10510286 | Matching Sentences:
[ Sen. 2, subscore: 1.00 ]: Characterization was done on the sugar chains of glutelin , a major storage protein in rice seeds . The basic subunits of glutelin were shown to be glycoproteins by staining with PAS and the lectins concanavalin A ( Con A ) and peanut agglutinin ( PNA ) . The binding of PNA to the basic subunits was substantially reduced by treatment of the glutelin with NaIO4 , NaOH , or O-glycanase . The sugar chains of the subunits , obtained by hydrazinolysis and O-glycanase , were pyridylaminated and subjected to 2-dimensional HPLC analysis using C ( 18 ) and acrylamide-derivatized columns . It was found that the Galbeta-1 , 3GalNAc disaccharide , which was previously identified as a core 1 structure of mucin-type sugar chains , is conjugated to the glutelin subunits . Furthermore , amino acid sequencing of an 11-kDa peptide of the subunits , recognized by both PNA and Con A , suggested that both N-linked and O-linked glycosylation occurs in the carboxy-terminal region of these subunits .
[ Sen. 3, subscore: 1.00 ]: Characterization was done on the sugar chains of glutelin , a major storage protein in rice seeds . The basic subunits of glutelin were shown to be glycoproteins by staining with PAS and the lectins concanavalin A ( Con A ) and peanut agglutinin ( PNA ) . The binding of PNA to the basic subunits was substantially reduced by treatment of the glutelin with NaIO4 , NaOH , or O-glycanase . The sugar chains of the subunits , obtained by hydrazinolysis and O-glycanase , were pyridylaminated and subjected to 2-dimensional HPLC analysis using C ( 18 ) and acrylamide-derivatized columns . It was found that the Galbeta-1 , 3GalNAc disaccharide , which was previously identified as a core 1 structure of mucin-type sugar chains , is conjugated to the glutelin subunits . Furthermore , amino acid sequencing of an 11-kDa peptide of the subunits , recognized by both PNA and Con A , suggested that both N-linked and O-linked glycosylation occurs in the carboxy-terminal region of these subunits .
[ Sen. 6, subscore: 1.00 ]: Characterization was done on the sugar chains of glutelin , a major storage protein in rice seeds . The basic subunits of glutelin were shown to be glycoproteins by staining with PAS and the lectins concanavalin A ( Con A ) and peanut agglutinin ( PNA ) . The binding of PNA to the basic subunits was substantially reduced by treatment of the glutelin with NaIO4 , NaOH , or O-glycanase . The sugar chains of the subunits , obtained by hydrazinolysis and O-glycanase , were pyridylaminated and subjected to 2-dimensional HPLC analysis using C ( 18 ) and acrylamide-derivatized columns . It was found that the Galbeta-1 , 3GalNAc disaccharide , which was previously identified as a core 1 structure of mucin-type sugar chains , is conjugated to the glutelin subunits . Furthermore , amino acid sequencing of an 11-kDa peptide of the subunits , recognized by both PNA and Con A , suggested that both N-linked and O-linked glycosylation occurs in the carboxy-terminal region of these subunits .
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Score: 6.00 |
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| Title: Developmentally regulated expression of a peptide : N-glycanase during germination of rice seeds ( Oryza sativa ) and its purification and characterization .
| | Author: Chang T Kuo MC Khoo KH Inoue S Inoue Y | | Journal: J Biol . Chem . Citation: V : 275 ( 1 ) P : 129-34 Year: 2000 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10617595 Accession (PMID): 10617595 | Matching Sentences:
[ Sen. 1, subscore: 1.00 ]: Peptide : N-glycanase ( PNGase ; EC 3 . 5 . 1 . 52 ) activity was detected in dormant rice seeds ( Oryza sativa ) and the imbibed rice grains . Time-course studies revealed that the enzyme activity remained almost constant until about 30 h after imbibition in both of endosperm and embryo it issue-containing areas , and started to increase only in growing germ part , reached a peak at about 3-day stage , followed by a gradual decrease concomitant with a sharp increase in the coleoptile . The specific activity increased about 6-fold at about 3-day stage . PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h , and the apparent molecular weight of the purified enzyme , estimated by SDS-polyacrylamide gel electrophoresis ( SDS-PAGE ) , was about 80 , 000 . The purified enzyme was designated PNGase Os to denote its origin . The N-terminal sequence of the 10 residues was determined to be SYNVASVAGL . The purified PNGase Os in SDS-PAGE appeared as a rather broad band , consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column . PNGase expressed in coleoptile under anoxia condition was also purified , and both of the purified enzymes were found to exhibit very similar , if not identical , electrophoretic mobility in SDS-PAGE . PNGase Os exhibited a broad pH-activity profile with an optimum of 4-5 and , interestingly , was significantly inactivated by K ( + ) and Na ( + ) at near the physiological concentration , 100 mM . These results are discussed in relation to other work .
[ Sen. 4, subscore: 1.00 ]: Peptide : N-glycanase ( PNGase ; EC 3 . 5 . 1 . 52 ) activity was detected in dormant rice seeds ( Oryza sativa ) and the imbibed rice grains . Time-course studies revealed that the enzyme activity remained almost constant until about 30 h after imbibition in both of endosperm and embryo it issue-containing areas , and started to increase only in growing germ part , reached a peak at about 3-day stage , followed by a gradual decrease concomitant with a sharp increase in the coleoptile . The specific activity increased about 6-fold at about 3-day stage . PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h , and the apparent molecular weight of the purified enzyme , estimated by SDS-polyacrylamide gel electrophoresis ( SDS-PAGE ) , was about 80 , 000 . The purified enzyme was designated PNGase Os to denote its origin . The N-terminal sequence of the 10 residues was determined to be SYNVASVAGL . The purified PNGase Os in SDS-PAGE appeared as a rather broad band , consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column . PNGase expressed in coleoptile under anoxia condition was also purified , and both of the purified enzymes were found to exhibit very similar , if not identical , electrophoretic mobility in SDS-PAGE . PNGase Os exhibited a broad pH-activity profile with an optimum of 4-5 and , interestingly , was significantly inactivated by K ( + ) and Na ( + ) at near the physiological concentration , 100 mM . These results are discussed in relation to other work .
[ Sen. 5, subscore: 1.00 ]: Peptide : N-glycanase ( PNGase ; EC 3 . 5 . 1 . 52 ) activity was detected in dormant rice seeds ( Oryza sativa ) and the imbibed rice grains . Time-course studies revealed that the enzyme activity remained almost constant until about 30 h after imbibition in both of endosperm and embryo it issue-containing areas , and started to increase only in growing germ part , reached a peak at about 3-day stage , followed by a gradual decrease concomitant with a sharp increase in the coleoptile . The specific activity increased about 6-fold at about 3-day stage . PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h , and the apparent molecular weight of the purified enzyme , estimated by SDS-polyacrylamide gel electrophoresis ( SDS-PAGE ) , was about 80 , 000 . The purified enzyme was designated PNGase Os to denote its origin . The N-terminal sequence of the 10 residues was determined to be SYNVASVAGL . The purified PNGase Os in SDS-PAGE appeared as a rather broad band , consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column . PNGase expressed in coleoptile under anoxia condition was also purified , and both of the purified enzymes were found to exhibit very similar , if not identical , electrophoretic mobility in SDS-PAGE . PNGase Os exhibited a broad pH-activity profile with an optimum of 4-5 and , interestingly , was significantly inactivated by K ( + ) and Na ( + ) at near the physiological concentration , 100 mM . These results are discussed in relation to other work .
[ Sen. 7, subscore: 1.00 ]: Peptide : N-glycanase ( PNGase ; EC 3 . 5 . 1 . 52 ) activity was detected in dormant rice seeds ( Oryza sativa ) and the imbibed rice grains . Time-course studies revealed that the enzyme activity remained almost constant until about 30 h after imbibition in both of endosperm and embryo it issue-containing areas , and started to increase only in growing germ part , reached a peak at about 3-day stage , followed by a gradual decrease concomitant with a sharp increase in the coleoptile . The specific activity increased about 6-fold at about 3-day stage . PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h , and the apparent molecular weight of the purified enzyme , estimated by SDS-polyacrylamide gel electrophoresis ( SDS-PAGE ) , was about 80 , 000 . The purified enzyme was designated PNGase Os to denote its origin . The N-terminal sequence of the 10 residues was determined to be SYNVASVAGL . The purified PNGase Os in SDS-PAGE appeared as a rather broad band , consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column . PNGase expressed in coleoptile under anoxia condition was also purified , and both of the purified enzymes were found to exhibit very similar , if not identical , electrophoretic mobility in SDS-PAGE . PNGase Os exhibited a broad pH-activity profile with an optimum of 4-5 and , interestingly , was significantly inactivated by K ( + ) and Na ( + ) at near the physiological concentration , 100 mM . These results are discussed in relation to other work .
[ Sen. 8, subscore: 1.00 ]: Peptide : N-glycanase ( PNGase ; EC 3 . 5 . 1 . 52 ) activity was detected in dormant rice seeds ( Oryza sativa ) and the imbibed rice grains . Time-course studies revealed that the enzyme activity remained almost constant until about 30 h after imbibition in both of endosperm and embryo it issue-containing areas , and started to increase only in growing germ part , reached a peak at about 3-day stage , followed by a gradual decrease concomitant with a sharp increase in the coleoptile . The specific activity increased about 6-fold at about 3-day stage . PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h , and the apparent molecular weight of the purified enzyme , estimated by SDS-polyacrylamide gel electrophoresis ( SDS-PAGE ) , was about 80 , 000 . The purified enzyme was designated PNGase Os to denote its origin . The N-terminal sequence of the 10 residues was determined to be SYNVASVAGL . The purified PNGase Os in SDS-PAGE appeared as a rather broad band , consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column . PNGase expressed in coleoptile under anoxia condition was also purified , and both of the purified enzymes were found to exhibit very similar , if not identical , electrophoretic mobility in SDS-PAGE . PNGase Os exhibited a broad pH-activity profile with an optimum of 4-5 and , interestingly , was significantly inactivated by K ( + ) and Na ( + ) at near the physiological concentration , 100 mM . These results are discussed in relation to other work .
[ Sen. 9, subscore: 1.00 ]: Peptide : N-glycanase ( PNGase ; EC 3 . 5 . 1 . 52 ) activity was detected in dormant rice seeds ( Oryza sativa ) and the imbibed rice grains . Time-course studies revealed that the enzyme activity remained almost constant until about 30 h after imbibition in both of endosperm and embryo it issue-containing areas , and started to increase only in growing germ part , reached a peak at about 3-day stage , followed by a gradual decrease concomitant with a sharp increase in the coleoptile . The specific activity increased about 6-fold at about 3-day stage . PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h , and the apparent molecular weight of the purified enzyme , estimated by SDS-polyacrylamide gel electrophoresis ( SDS-PAGE ) , was about 80 , 000 . The purified enzyme was designated PNGase Os to denote its origin . The N-terminal sequence of the 10 residues was determined to be SYNVASVAGL . The purified PNGase Os in SDS-PAGE appeared as a rather broad band , consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column . PNGase expressed in coleoptile under anoxia condition was also purified , and both of the purified enzymes were found to exhibit very similar , if not identical , electrophoretic mobility in SDS-PAGE . PNGase Os exhibited a broad pH-activity profile with an optimum of 4-5 and , interestingly , was significantly inactivated by K ( + ) and Na ( + ) at near the physiological concentration , 100 mM . These results are discussed in relation to other work .
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Score: 2.00 |
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| Title: Genotypic characterization of drug-resistant Mycobacterium tuberculosis isolates from Peru .
| | Author: Escalante P Ramaswamy S Sanabria H Soini H Pan X Valiente-Castillo O Musser JM .
| | Journal: Tuber .
Lung Dis .
Citation: V : 79 ( 2 ) P : 111-8 Year: Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10645449 Accession (PMID): 10645449 | Matching Sentences:
[ Sen. 3, subscore: 1.00 ]: SETTING : Twenty-nine epidemiological unrelated and mostly multidrug-resistant Mycobacterium tuberculosis ( MDR-TB ) strains from Peruvian patients . OBJECTIVE : To investigate the molecular genetics of MDR-TB strains recovered in a Latin American country . DESIGN : Antimicrobial agent susceptibility testing , major genetic group designation , IS6110 fingerprinting , spoligotyping , and automated deoxyribonucleic acid sequencing of regions of the katG , rpoB , embB , gyrA , and pncA genes with mutations commonly associated with drug resistance . RESULTS : Nineteen isolates were found to be multidrug-resistant by susceptibility testing . IS6110 typing showed that virtually all isolates were unique and therefore had independently acquired drug resistance . Seventy-nine percent of isoniazid-resistant strains had a Ser315Thr amino acid change in KatG . Ninety-five percent of rifampin-resistant isolates had amino acid replacements in the rifampin-resistance determining region of RpoB . Six of 11 ethambutol-resistant strains had EmbB alterations . Eleven pyrazinamide-resistant strains had distinct mutations in pncA . CONCLUSION : Virtually all organisms evolved drug resistance independently . The types of drug resistance-associated mutations identified were very similar to changes occurring in isolates from other areas of the world . Nucleotide sequence-based strategies for rapid detection of drug resistance-conferring mutants will be applicable to organisms recovered in Peru , and potentially other areas of Latin America .
[ Sen. 9, subscore: 1.00 ]: SETTING : Twenty-nine epidemiological unrelated and mostly multidrug-resistant Mycobacterium tuberculosis ( MDR-TB ) strains from Peruvian patients . OBJECTIVE : To investigate the molecular genetics of MDR-TB strains recovered in a Latin American country . DESIGN : Antimicrobial agent susceptibility testing , major genetic group designation , IS6110 fingerprinting , spoligotyping , and automated deoxyribonucleic acid sequencing of regions of the katG , rpoB , embB , gyrA , and pncA genes with mutations commonly associated with drug resistance . RESULTS : Nineteen isolates were found to be multidrug-resistant by susceptibility testing . IS6110 typing showed that virtually all isolates were unique and therefore had independently acquired drug resistance . Seventy-nine percent of isoniazid-resistant strains had a Ser315Thr amino acid change in KatG . Ninety-five percent of rifampin-resistant isolates had amino acid replacements in the rifampin-resistance determining region of RpoB . Six of 11 ethambutol-resistant strains had EmbB alterations . Eleven pyrazinamide-resistant strains had distinct mutations in pncA . CONCLUSION : Virtually all organisms evolved drug resistance independently . The types of drug resistance-associated mutations identified were very similar to changes occurring in isolates from other areas of the world . Nucleotide sequence-based strategies for rapid detection of drug resistance-conferring mutants will be applicable to organisms recovered in Peru , and potentially other areas of Latin America .
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Score: 2.00 |
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| Title: Sequence analysis of Pns11 , a nonstructural protein of rice gall dwarf virus , and its expression and detection in infected rice plants and vector insects .
| | Author: Moriyasu Y Ishikawa K Kikuchi A Imanishi S Tomita S Akutsu K Omura T | | Journal: Virus Genes Citation: V : 20 ( 3 ) P : 237-41 Year: Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10949951 Accession (PMID): 10949951 | Matching Sentences:
[ Sen. 2, subscore: 1.00 ]: The nucleotide sequence of genome segment S11 of rice gall dwarf virus ( RGDV ) , a member of Phytoreovirus , was determined . The segment encodes a putative protein of 40 kDa that exhibits approximately 37% homology at the amino acid level to the nonstructural proteins Pns10 of rice dwarf and wound tumor viruses , which are other members of Phytoreovirus . A band of a protein with an apparent molecular mass of 40 kDa was specifically detected in an analysis of cells transfected with S11 cDNA . An antiserum raised against this protein reacted with a protein of approximately 40kDa after fractionation by SDS-PAGE of materials prepared from infected plants and from viruliferous vector insects . However , the antiserum did not react with purified viral proteins . These results suggest that S11 encodes a nonstructural protein of RGDV . This protein was named Pns11 .
[ Sen. 7, subscore: 1.00 ]: The nucleotide sequence of genome segment S11 of rice gall dwarf virus ( RGDV ) , a member of Phytoreovirus , was determined . The segment encodes a putative protein of 40 kDa that exhibits approximately 37% homology at the amino acid level to the nonstructural proteins Pns10 of rice dwarf and wound tumor viruses , which are other members of Phytoreovirus . A band of a protein with an apparent molecular mass of 40 kDa was specifically detected in an analysis of cells transfected with S11 cDNA . An antiserum raised against this protein reacted with a protein of approximately 40kDa after fractionation by SDS-PAGE of materials prepared from infected plants and from viruliferous vector insects . However , the antiserum did not react with purified viral proteins . These results suggest that S11 encodes a nonstructural protein of RGDV . This protein was named Pns11 .
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