scholarly journals Nucleotide sequence and deduced amino acid sequence of a new Lepidoptera-specific crystal protein gene fromBacillus thuringiensis

1990 ◽  
Vol 18 (18) ◽  
pp. 5545-5545 ◽  
Author(s):  
Herman Höfte ◽  
Piet Soetaert ◽  
Stefan Jansens ◽  
Marnix Peferoen
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Protein Gene ◽  
Crystal Protein

scholarly journals Biological, Pathological, and Molecular Characteristics of a New Potyvirus, Dendrobium Chlorotic Mosaic Virus, Infecting Dendrobium Orchid

Plant Disease ◽  
2019 ◽  
Vol 103 (7) ◽  
pp. 1605-1612 ◽  
Author(s):  
Chih-Hung Huang ◽  
Chia-Hsing Tai ◽  
Ruey-Song Lin ◽  
Chung-Jan Chang ◽  
Fuh-Jyh Jan
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Mosaic Virus ◽  
Coat Protein Gene ◽  
Nucleotide Sequence Identity ◽  
Amino Acid Sequence Identity ◽  
Protein Gene ◽  
Sequence Identity

Dendrobium smillieae is one of the popular orchids in Taiwan. This report describes a new potyvirus tentatively named Dendrobium chlorotic mosaic virus (DeCMV) causing chlorotic and mosaic symptoms in D. smillieae. Enzyme-linked immunosorbent assay (ELISA) tests using six antisera against orchid-infecting viruses revealed that only a monoclonal antibody against the potyvirus group reacted positively with crude saps prepared from a symptomatic dendrobium orchid. Potyvirus-like, flexuous, filamentous particles were observed under an electron microscope, measuring approximately 700 to 800 nm in length and 11 to 12 nm in diameter. Sequence analyses revealed that DeCMV coat protein gene shared 59.6 to 66.0% nucleotide sequence identity and 57.6 to 66.0% amino acid sequence identity, whereas the DeCMV complete genome shared 54.1 to 57.3% nucleotide sequence identity and 43.7 to 49.5% amino acid sequence identity with those other known potyviruses. These similarity levels were much lower than the criteria set for species demarcation in potyviruses. Thus, DeCMV can be considered a new potyvirus. The whole DeCMV genome contains 10,041 nucleotides (GenBank accession no. MK241979) and encodes a polyprotein that is predicted to produce 10 proteins by proteolytic cleavage. In a pathogenicity test, results of inoculation assays demonstrated that DeCMV can be transmitted to dendrobium orchids by grafting and mechanical inoculation, as verified by ELISA and western blot analyses using the DeCMV polyclonal antiserum and by reverse transcription polymerase chain reaction using the coat protein gene-specific primers. The inoculated orchids developed similar chlorotic and mosaic symptoms. In conclusion, DeCMV is a novel orchid-infecting potyvirus, and this is the first report of a new potyvirus that infects dendrobium orchids in Taiwan.

scholarly journals Nucleotide sequence of the coat protein gene of the Skierniewice isolate of plum pox virus (PPV).

1994 ◽  
Vol 41 (1) ◽  
pp. 87-95 ◽  
Author(s):  
K Wypijewski ◽  
T Malinowski ◽  
W Musiał ◽  
J Augustyniak
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Protein Gene ◽  
Plum Pox Virus ◽  
Rt Pcr ◽  
Chain Reaction ◽  
Polymerase Chain ◽  
Very High

The coat protein (CP) gene of the Skierniewice isolate of plum pox virus (PPV-S) has been amplified using the reverse transcription--polymerase chain reaction (RT-PCR), cloned and sequenced. The nucleotide sequence of the gene and the deduced amino-acid sequence of PPV-S CP were compared with those of other PPV strains. The nucleotide sequence showed very high homology to most of the published sequences. The motif: Asp-Ala-Gly (DAG), important for the aphid transmissibility, was present in the amino-acid sequence. Our isolate did not react in ELISA with monoclonal antibodies MAb06 supposed to be specific for PPV-D.

scholarly journals Nucleotide sequence of the melB gene and characteristics of deduced amino acid sequence of the melibiose carrier in Escherichia coli.

1984 ◽  
Vol 259 (7) ◽  
pp. 4320-4326 ◽  
Author(s):  
H Yazyu ◽  
S Shiota-Niiya ◽  
T Shimamoto ◽  
H Kanazawa ◽  
M Futai ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence

scholarly journals Terminal deoxynucleotidyltransferase. Alignment of α- and β-subunits of the core enzyme along the primary translation product

1985 ◽  
Vol 227 (3) ◽  
pp. 1003-1007 ◽  
Author(s):  
C M Beach ◽  
S K Chan ◽  
T C Vanaman ◽  
M S Coleman
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Beta Subunits ◽  
Isolation And Purification ◽  
C Terminus ◽  
Human Lymphoblast ◽  
Catalytically Active ◽  
Single Polypeptide ◽  
Dna Nucleotide Sequence

Terminal deoxynucleotidyltransferase exists in multiple Mr forms, all apparently generated from a single polypeptide of 62kDa. On isolation and purification, the smallest catalytically active protein of this enzyme consists of two subunits, alpha (12kDa) and beta (30kDa). Recently a complementary-DNA nucleotide sequence has been reported for a portion of the enzyme from human lymphoblast. We have pinpointed the locations of the alpha- and beta-subunits within the elucidated nucleotide sequence. From these data, the portions of the nucleotide sequence coding for the catalytically important area of the transferase can be estimated. Here the amino acid sequence of a number of tryptic peptides from calf alpha- and beta-subunits is presented. Because of the striking homology between the amino acid sequence of the calf enzyme and that predicted for human lymphoblast enzyme, it is possible for us to conclude that the alpha-subunit was generated from the C-terminus of the precursor protein and the beta-subunit was non-overlapping and proximal.

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