A New Allele, DNASE16, of Human Deoxyribonuclease I Polymorphism Encodes an Arg to Cys Substitution Responsible for Its Instability

A new allele, DNASE1*6, of human deoxyribonuclease I (DNase I) has been discovered by isoelectric focusing: its gene product has the most cathodic pI of the six electrophoretic variants. Results of DNA sequencing, mismatched PCR-restriction fragment length polymorphism, and transient transfection of...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1999-06, Vol.260 (1), p.280-283
Main Authors: Yasuda, Toshihiro, Takeshita, Haruo, Iida, Reiko, Kogure, Shinya, Kishi, Koichiro
Format: Article
Language:English
Subjects:
Alleles
Amino Acid Sequence
Animals
Arginine - genetics
Base Sequence
COS Cells
Cystine - genetics
Deoxyribonuclease I - genetics
Humans
Molecular Sequence Data
Polymorphism, Restriction Fragment Length
Time Factors
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Summary:A new allele, DNASE1*6, of human deoxyribonuclease I (DNase I) has been discovered by isoelectric focusing: its gene product has the most cathodic pI of the six electrophoretic variants. Results of DNA sequencing, mismatched PCR-restriction fragment length polymorphism, and transient transfection of the variant construct showed that the mutant was caused by a C–T transition at nucleotide position 1826, resulting in an Arg to Cys substitution at amino acid position 185 of the mature enzyme. The variant isoenzyme, expressed in COS-7 cells, was more labile than the other types. Instability and an increase in the pI value of the variant suggest that a structural alteration, perhaps due to aberrant formation of a disulfide bond, could occur in the enzyme.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1999.0900