Escherichia coli signal peptidase recognizes and cleaves archaeal signal sequence View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2017-07

AUTHORS

Majida Atta Muhammad, Samia Falak, Naeem Rashid, Qurra-tul-Ann Afza Gardner, Nasir Ahmad, Tadayuki Imanaka, Muhammad Akhtar

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. More... »

PAGES

821-825

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s0006297917070070

DOI

http://dx.doi.org/10.1134/s0006297917070070

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1090861299

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28918746


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