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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-11-14
pubmed:abstractText
Two genes encoding the 32- and 40-kDa polypeptides of Bacillus thuringiensis strain 90-F-45-14 crystals were cloned, expressed in an acrystalliferous B. thuringiensis strain, and sequenced. The polypeptides had deduced molecular weights of 30,319 and 33,885, respectively. The amino acid sequence of the 32-kDa protein was 37.7% identical to the known sequence of a non-insecticidal parasporal protein in B. thuringiensis serovar thompsoni crystals. The sequence of the cloned 40-kDa protein was 37.0% and 22.3% identical to that of the existing Cry protein classes, Cry15Aa1 and Cry23Aa1, respectively. Thus, this protein constitutes a novel protein class, Cry33Aa1. The open reading frames of the two genes were located on the predominant plasmid of 17,629 bp (=11,752 MDa) in the same orientation, and they were separated by the sequence of 32 nucleotides. The two proteins are likely produced simultaneously from a single transcript to form spherical crystals.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0343-8651
pubmed:author
pubmed:issnType
Print
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Cloning and characterization of two novel crystal protein genes from a Bacillus thuringiensis serovar dakota strain.
pubmed:affiliation
Biotechnology & Food Research Institute, Fukuoka Industrial Technology Center, Aikawa-machi 1465-5 Kurume, Fukuoka 839-0861, Japan.
pubmed:publicationType
Journal Article