Molecular cloning and characterization of gene encoding novel puromycin-inactivating enzyme from blasticidin S-producing Streptomyces morookaensis
Section snippets
Bacterial strains, plasmids, and cultivation media
BS-producing S. morookaensis JCM 4673 (= KCC S-0673) was obtained from the Japan Collection of Microorganisms (JCM) at the Institute of Physical and Chemical Research, Wako. The spores, formed on a YEME medium (1% glucose, 0.5% Polypepton, 0.3% yeast extract, 0.3% malt extract, and 0.04% MgCl2·6H2O, pH 7.0) supplemented with 1.5% agar, were suspended in 0.85% NaCl containing 20% glycerol and stored at −70°C until use. The Streptomyces spores were inoculated and cultured in a YEME medium
Cloning of gene for PMH
Streptomyces genes, in general, have a strong preference for utilizing codons that contain G or C in the third position (18). This bias was reflected in the design and synthesis of the mixed oligonucleotides corresponding to the N-terminal amino acid sequence (4A-P-Y-G-A-W-Q-S-P-I-14D) (9) of PMH from S. morookaensis JCM4673. The mixed probes, labeled with fluorescein, had a GCICCITACGGIGCITGGCAIWSICCI ATCGAC sequence (where W is A or T, I is deoxyinosine, and S is C or G). The probes were
References (33)
- et al.
Acetylation of puromycin by Streptomyces alboniger, the producing organism
Biochem. Biophys. Res. Commun.
(1983) - et al.
Blasticidin S-producing Streptomyces morookaensis possesses an enzyme activity which hydrolyzes puromycin
FEMS Microbiol. Lett.
(1995) - et al.
Bleomycin hydrolase is a unique thiol aminopeptidase
Biochem. Biophys. Res. Commun.
(1989) - et al.
Protein measurement with the Folin phenol reagent
J. Biol. Chem.
(1951) - et al.
The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences
Gene
(1984) - et al.
Prokaryotic promoters in biotechnology
Biotechnol. Annu. Rev.
(1995) - et al.
Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases
J. Biol. Chem.
(1993) - et al.
Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding
J. Mol. Biol.
(2004) - et al.
The noncatalytic beta-propeller domain of prolyl oligopeptidase enhances the catalytic capability of the peptidase domain
J. Biol. Chem.
(2000) - et al.
Tricorn protease (TRI) interacting factor 1 from Thermoplasma acidophilum is a proline iminopeptidase
FEBS Lett.
(1996)
BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase
J. Biol. Chem.
Catalytic properties of the cysteine aminopeptidase PepC, a bacterial bleomycin hydrolase
Biochim. Biophys. Acta
Achromycin: a new antibiotic having trypanocidal properties
Antibiot. Chemother.
Proton magnetic resonance of purine and pyrimidine derivatives. X. The conformation of puromycin
J. Am. Chem. Soc.
Amino acid transfer from aminoacyl-ribonucleic acids to protein on ribosomes of Escherichia coli
Proc. Natl. Acad. Sci. USA
Mechanism of self-protection in a puromycin-producing micro-organism
J. Gen. Microbiol.
Cited by (11)
Aminolytic reaction catalyzed by d-stereospecific amidohydrolases from Streptomyces spp
2011, BiochimieCitation Excerpt :A similar phenomenon was observed in a family S9 aminopeptidase from Streptomyces [14,15]; the enzyme can synthesize β-Ala containing peptides and diverse prolyl peptides. Family S9 aminopeptidase has catalytic Ser residue in its active centers [36,37]; it shows an aminolysis reaction. Family S9 aminopeptidase from Streptomyces cannot hydrolyze carnosine (β-Ala-His), but it can synthesize carnosine efficiently by its aminolytic reaction [14].
β-Alanyl peptide synthesis by Streptomyces S9 aminopeptidase
2010, Journal of BiotechnologyPutative "acylaminoacyl" peptidases from Streptomyces griseus and S. coelicolor display "aminopeptidase" activities with distinct substrate specificities and sensitivities to reducing reagent
2009, Biochimica et Biophysica Acta - Proteins and ProteomicsAchieving functionality through modular build-up: Structure and size selection of serine oligopeptidases
2019, Current Protein and Peptide ScienceGene cloning and biochemical characterization of eryngase, a serine aminopeptidase of Pleurotus eryngii belonging to the family S9 peptidases
2014, Bioscience, Biotechnology and BiochemistryInactivation of chloramphenicol and florfenicol by a novel chloramphenicol hydrolase
2012, Applied and Environmental Microbiology