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Escherichia coli Signal Peptidases Cleave the Signal Sequence of TK0522, a Carbohydrate Esterase from Hyperthermophilic Archaeon Thermococcus kodakarensis

Escherichia coli Signal Peptidases Cleave the Signal Sequence of TK0522, a Carbohydrate Esterase from Hyperthermophilic Archaeon Thermococcus kodakarensis

Anam Tariq, Alina Gul, Majida Atta Muhammad, Samia Falak and Naeem Rashid*

School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore 54590, Pakistan

*      Corresponding author: naeem.ff.sbs @pu.edu.pk; [email protected]

 

ABSTRACT

TK0522 gene, encoding a carbohydrate esterase, from Thermococcus kodakarensis was cloned with its native signal sequence and expressed in Escherichia coli. Heterologous gene expression resulted in production of recombinant protein in the cytoplasm which secreted gradually to the extracellular culture medium. Determination of the N-terminal amino acid sequence of the recombinant protein, in the extracellular medium, revealed that the 19 amino acid signal peptide was cleaved between Ala19 and Gly20. It seems probable that the signal peptide of TK0522 can be used for secretion of other recombinant proteins produced in E. coli.

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Pakistan Journal of Zoology

October

Pakistan J. Zool., Vol. 56, Iss. 5, pp. 2001-2500

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