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Escherichia coli signal peptidase recognizes and cleaves archaeal signal sequence
- Source :
- Biochemistry (Moscow). 82:821-825
- Publication Year :
- 2017
- Publisher :
- Pleiades Publishing Ltd, 2017.
-
Abstract
- Tk1884, an open reading frame encoding α-amylase in Thermococcus kodakarensis, was cloned with the native signal sequence and expressed in Escherichia coli. Heterologous gene expression resulted in secretion of the recombinant protein to the extracellular culture medium. Extracellular α-amylase activity gradually increased after induction. Tk1884 was purified from the extracellular medium, and its molecular mass determined by electrospray ionization mass spectrometry indicated the cleavage of a few amino acids. The N-terminal amino acid sequence of the purified Tk1884 was determined, which revealed that the signal peptide was cleaved between Ala26 and Ala27 by E. coli signal peptidase. To the best of our knowledge, this is the first report describing an archaeal signal sequence recognized and cleaved by E. coli signal peptidase.
- Subjects :
- 0301 basic medicine
Signal peptide
Spectrometry, Mass, Electrospray Ionization
Archaeal Proteins
Biophysics
medicine.disease_cause
Biochemistry
Biochemistry, Genetics and Molecular Biology (miscellaneous)
03 medical and health sciences
Bacterial Proteins
Escherichia coli
medicine
Cloning, Molecular
Peptide sequence
Enzyme Assays
chemistry.chemical_classification
Signal peptidase
030102 biochemistry & molecular biology
Molecular mass
biology
Serine Endopeptidases
Membrane Proteins
General Medicine
biology.organism_classification
Molecular biology
Recombinant Proteins
Thermococcus kodakarensis
Amino acid
Molecular Weight
Thermococcus
030104 developmental biology
chemistry
alpha-Amylases
Geriatrics and Gerontology
Signal peptide peptidase
Subjects
Details
- ISSN :
- 16083040 and 00062979
- Volume :
- 82
- Database :
- OpenAIRE
- Journal :
- Biochemistry (Moscow)
- Accession number :
- edsair.doi.dedup.....4402bb1effd94c1dbb40f29d7840f4d0