Nucleotide sequence and deduced amino acid sequence of a coleopteran-active delta-endotoxin gene from Bacillus thuringiensis subsp. san diego

Gene ◽  
1987 ◽  
Vol 57 (1) ◽  
pp. 37-46 ◽  
Author(s):  
Corinna Herrnstadt ◽  
Thomas E. Gilroy ◽  
Donna A. Sobieski ◽  
Brian D. Bennett ◽  
Frank H. Gaertner
Keyword(s):  
Amino Acid ◽  
Bacillus Thuringiensis ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
San Diego ◽  
Bacillus Thuringiensis Subsp ◽  
Delta Endotoxin

scholarly journals Proteolytic processing of a coleopteran-specific δ-endotoxin produced by Bacillus thuringiensis var. tenebrionis

1989 ◽  
Vol 261 (1) ◽  
pp. 99-105 ◽  
Author(s):  
J Carroll ◽  
J Li ◽  
D J Ellar
Keyword(s):  
Amino Acid ◽  
Bacillus Thuringiensis ◽  
Amino Acid Sequence ◽  
Proteinase Inhibitors ◽  
Cleavage Product ◽  
Proteolytic Processing ◽  
N Terminus ◽  
Delta Endotoxin ◽  
Insect Gut

Insecticidal protein delta-endotoxin crystals harvested from sporulated cultures of Bacillus thuringiensis var. tenebrionis contain a major polypeptide of 67 kDa and minor polypeptides of 73, 72, 55 and 46 kDa. During sporulation, only the 73 kDa polypeptide could be detected at stage I. The 67 kDa polypeptide was first detected at stage II and increased in concentration throughout the later stages of sporulation and after crystal release, with a concomitant decrease in the 73 kDa polypeptide. This change could be blocked by the addition of proteinase inhibitors. Trypsin or insect-gut-extract treatment of the delta-endotoxin crystals after solubilization resulted in a cleavage product of 55 kDa with asparagine-159 of the deduced amino acid sequence of the toxin [Höfte, Seurinck, van Houtven & Vaeck (1987) Nucleic Acids Res. 15, 71-83; Sekar, Thompson, Maroney, Bookland & Adang (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 7036-7040; McPherson, Perlak, Fuchs, Marrone, Lavrik & Fischhoff (1988) Biotechnology 6, 61-66] at the N-terminus. This polypeptide was found to be as toxic in vivo as native delta-endotoxin.

scholarly journals Characterization of cry1Cb3 and cry1Fb7 from Bacillus thuringiensis subsp. galleriae

2015 ◽  
Vol 10 (1) ◽  
Author(s):  
Tianpei Huang ◽  
Ying Xiao ◽  
Jieru Pan ◽  
Lingling Zhang ◽  
Ivan Gelbič ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Bacillus Thuringiensis ◽  
Amino Acid Sequence ◽  
Amino Acid Residues ◽  
Reading Frame ◽  
Bacillus Thuringiensis Subsp ◽  
Calculated Molecular Weight ◽  
Pcr Rflp ◽  
Genes Encoding

AbstractTwo cry1-type genes encoding insecticidal crystal proteins (ICPs) were detected by PCR-RFLP and cloned from Bacillus thuringiensis subsp. galleriae 87. The nucleotide sequences were deposited in GenBank with accession numbers EU679501 and EU679502, and designated as cry1Fb7 and cry1Cb3 respectively by B. thuringiensis Delta- Endotoxin Nomenclature Committee. cry1Cb3 shared 99% homology with other cry1Cb genes. The existence of two additional stop codons indicated cry1Cb3 was a silent gene. The cry1Cb3 was 3531 bp with 38.98% G+C content and its first open reading frame (ORF) encoded a protein of 213 amino acid residues with a calculated molecular weight of 23.8 kDa and a predicted pI value of 4.63. Five amino acid sequence blocks (block 1, block 2, block 3, block 4 and block 5) were found in Cry1Cb3. Translation of cry1Fb7 revealed an ORF of 3525 bp with 39.12% G+C content and a protein with a calculated molecular weight of 133.2 kDa and a predicted pI value of 5.18. Cry1Fb7 had five amino acid sequence blocks (blocks 1, 2, 3, 4 and 5) and three domains (I, II and III), which consisted of 218 residues (Leu

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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