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EXPRESSION, PURIFICATION, AND CHARACTERIZATION OF A DROSOPHILA QC‐LIKE PROTEIN
Author(s) -
Parker Amanda Thigpen,
Bateman Robert C
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.1043.1
Subject(s) - biochemistry , yeast , fusion protein , biology , drosophila (subgenus) , enzyme , homology (biology) , protein precursor , peptide sequence , chemistry , microbiology and biotechnology , amino acid , recombinant dna , gene
Glutaminyl cyclase, the enzyme responsible for N‐terminal pyroglutamyl residue formation, is found in a broad range of living species from yeast to humans. A BLAST analysis using the human glutaminyl cyclase protein sequence has revealed a family of QC‐like proteins in organism from human to Drosophila with high homology to glutaminyl cyclase in several organisms including humans. In Drosophila , the QC‐like protein and QC protein have greater than 53% sequence identity. The predicted tertiary structure among the two proteins is highly conserved. To investigate the function and structure of these QC‐like proteins, bacterial fusion proteins were developed for the Drosophila QC‐like protein containing a purification tag. Purification resulted in a 40 kD protein which was apparently devoid of glutaminyl cyclase activity. Currently Drosophila QC and QC‐like proteins are being expressed in parallel to clarify their structural and functional relationship.