Cloning of a novel crystal protein gene cry1K from Bacillus thuringiensis subsp. morrisoni. 1995

B T Koo, and S H Park, and S K Choi, and B S Shin, and J I Kim, and J H Yu
Korea Research Institute of Bioscience and Biotechnology, KIST, Yusong, Taejon, South Korea.

A novel crystal protein gene cry1K has been cloned and sequenced from a Bacillus thuringiensis subsp. morrisoni BF190 isolated from phylloplane. The upstream promoter region of cry1K was almost identical with that of cry1B. The deduced amino acid sequence of Cry1K contains 1215 amino acid residues with an estimated molecular mass of 137 kDa. Comparison of the amino acid sequence of the Cry1K with that of Cry proteins revealed that Cry1K is most closely related to Cry1B and Cry1I. Cry1K has a high degree of identity with Cry1B in the region between initiator codon and conserved sequence block 1, and with Cry1F in the region between conserved block 3 and 5. Protein inclusion purified from a recombinant strain of B. thuringiensis expressing the cry1K gene was found to have a different insect-host specificity from Cry1B, Cry1I and Cry1F, Cry1K was found to be selectively toxic to Artogeia rapae and not active to Plutella xylostella.

UI MeSH Term Description Entries
D007313 Insecta Members of the phylum ARTHROPODA composed or organisms characterized by division into three parts: head, thorax, and abdomen. They are the dominant group of animals on earth with several hundred thousand different kinds. Three orders, HEMIPTERA; DIPTERA; and SIPHONAPTERA; are of medical interest in that they cause disease in humans and animals. (From Borror et al., An Introduction to the Study of Insects, 4th ed, p1). Insects,Insect
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010572 Pest Control, Biological Use of naturally-occuring or genetically-engineered organisms to reduce or eliminate populations of pests. Biological Pest Control,Biologic Pest Control,Pest Control, Biologic,Biologic Pest Controls,Biological Pest Controls,Pest Controls, Biologic,Pest Controls, Biological
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004269 DNA, Bacterial Deoxyribonucleic acid that makes up the genetic material of bacteria. Bacterial DNA
D004731 Endotoxins Toxins closely associated with the living cytoplasm or cell wall of certain microorganisms, which do not readily diffuse into the culture medium, but are released upon lysis of the cells. Endotoxin
D005798 Genes, Bacterial The functional hereditary units of BACTERIA. Bacterial Gene,Bacterial Genes,Gene, Bacterial
D006460 Hemolysin Proteins Proteins from BACTERIA and FUNGI that are soluble enough to be secreted to target ERYTHROCYTES and insert into the membrane to form beta-barrel pores. Biosynthesis may be regulated by HEMOLYSIN FACTORS. Hemolysin,Hemolysins,Hemalysins,Proteins, Hemolysin
D000083722 Bacillus thuringiensis Toxins Endotoxins produced by BACILLUS THURINGIENSIS used in transgenic plants and insecticides. When eaten by a susceptible insect they are protease activated in the insect midgut resulting in death from bacterial septicemia. B thuringiensis Toxins,B. thuringiensis Toxins,Bt Toxin,Bt Toxins,Toxin, Bt,Toxins, B thuringiensis,Toxins, B. thuringiensis
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

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