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MXNL06000069A - System for expressing and transporting recombinant proteins to the escherichia coli periplasm using the tat (twin-arginine translocation) secretion pathway. - Google Patents

System for expressing and transporting recombinant proteins to the escherichia coli periplasm using the tat (twin-arginine translocation) secretion pathway.

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Publication number
MXNL06000069A
MXNL06000069A MXNL06000069A MXNL06000069A MX NL06000069 A MXNL06000069 A MX NL06000069A MX NL06000069 A MXNL06000069 A MX NL06000069A MX NL06000069 A MXNL06000069 A MX NL06000069A
Authority
MX
Mexico
Prior art keywords
tat
escherichia coli
transport
coli periplasm
pathway
Prior art date
Application number
Other languages
Spanish (es)
Inventor
Ana Paulina Barba De La Rosa
Emilio Medina Rivero
Leandro Gabriel Ordonez Acevedo
Luz Maria Teresita Paz Maldonado
Victor Emmanuel Balderas Hernandez
Antonio De Leon-Rodriguez
Original Assignee
Inst Potosino De Investigacion
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Inst Potosino De Investigacion filed Critical Inst Potosino De Investigacion
Priority to MXNL06000069 priority Critical patent/MXNL06000069A/en
Publication of MXNL06000069A publication Critical patent/MXNL06000069A/en

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Abstract

The present invention describes an expression vector which contains a signal peptide using the Tat secretion pathway as an alternative of the Sec secretion system for the transport of cytoquinine and further proteins of biotechnological interest to Escherichia coli periplasm. The novel system consists in using the signal peptide of penicillin acylase (SPpac) which is mutated and fussed to the synthetic human interferon-y gene (hINF-y) for the transport of the protein to the Escherichia coli periplasm using the Tat pathway. The mutated SPpac includes the NdeI site at the 5¿ end, which is contained in the expression vector pEMR, at the 3¿ end the tryptophan codon being exchanged by the serine codon, thus generating the restriction site Hind III. The Leucine and Alanine codons are modified so as to generate the NheI site. Thus, two sites for restricting the cloning and fusion within a gene phase of homologous or heterologous proteins are generated. Nowadays there is no commercial vector available for the expression and transport of proteins, which include signal peptides using the Tat pathway.
MXNL06000069 2006-09-15 2006-09-15 System for expressing and transporting recombinant proteins to the escherichia coli periplasm using the tat (twin-arginine translocation) secretion pathway. MXNL06000069A (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
MXNL06000069 MXNL06000069A (en) 2006-09-15 2006-09-15 System for expressing and transporting recombinant proteins to the escherichia coli periplasm using the tat (twin-arginine translocation) secretion pathway.

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
MXNL06000069 MXNL06000069A (en) 2006-09-15 2006-09-15 System for expressing and transporting recombinant proteins to the escherichia coli periplasm using the tat (twin-arginine translocation) secretion pathway.

Publications (1)

Publication Number Publication Date
MXNL06000069A true MXNL06000069A (en) 2008-10-09

Family

ID=40941204

Family Applications (1)

Application Number Title Priority Date Filing Date
MXNL06000069 MXNL06000069A (en) 2006-09-15 2006-09-15 System for expressing and transporting recombinant proteins to the escherichia coli periplasm using the tat (twin-arginine translocation) secretion pathway.

Country Status (1)

Country Link
MX (1) MXNL06000069A (en)

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2016071707A1 (en) * 2014-11-07 2016-05-12 University Of Kent Biopharmaceutical production method
US12275685B2 (en) 2018-12-03 2025-04-15 Board Of Regents, The University Of Texas System Oligo-benzamide analogs and their use in cancer treatment

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2016071707A1 (en) * 2014-11-07 2016-05-12 University Of Kent Biopharmaceutical production method
US10457948B2 (en) 2014-11-07 2019-10-29 University Of Kent Biopharmaceutical production method
US12275685B2 (en) 2018-12-03 2025-04-15 Board Of Regents, The University Of Texas System Oligo-benzamide analogs and their use in cancer treatment

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