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Bovine gamma-interferon nuclear localization sequence provides translocation of recombinant protein to yeast Pichia pastoris cell nucleus. / Gradoboeva, A.E.; Padkina, M.V.

In: Cell and Tissue Biology, Vol. 4, No. 6, 2010, p. 566-571.

Research output: Contribution to journal › Article › peer-review

Harvard

Gradoboeva, AE & Padkina, MV 2010, 'Bovine gamma-interferon nuclear localization sequence provides translocation of recombinant protein to yeast Pichia pastoris cell nucleus', Cell and Tissue Biology, vol. 4, no. 6, pp. 566-571. https://doi.org/10.1134/S1990519X10060076

APA

Gradoboeva, A. E., & Padkina, M. V. (2010). Bovine gamma-interferon nuclear localization sequence provides translocation of recombinant protein to yeast Pichia pastoris cell nucleus. Cell and Tissue Biology, 4(6), 566-571. https://doi.org/10.1134/S1990519X10060076

Vancouver

Gradoboeva AE, Padkina MV. Bovine gamma-interferon nuclear localization sequence provides translocation of recombinant protein to yeast Pichia pastoris cell nucleus. Cell and Tissue Biology. 2010;4(6):566-571. https://doi.org/10.1134/S1990519X10060076

Author

Gradoboeva, A.E. ; Padkina, M.V. / Bovine gamma-interferon nuclear localization sequence provides translocation of recombinant protein to yeast Pichia pastoris cell nucleus. In: Cell and Tissue Biology. 2010 ; Vol. 4, No. 6. pp. 566-571.

BibTeX

@article{8a7b51803ab24109a2dead7cb3a8e441,
title = "Bovine gamma-interferon nuclear localization sequence provides translocation of recombinant protein to yeast Pichia pastoris cell nucleus",
abstract = "It is known that the expression of heterologous protein production in microorganisms has a negative influence on the host cell. Therefore, to utilize microorganisms for production of recombinant proteins it is necessary the follow the fate of recombinant proteins in cells. In this study, we constructed a modified bovine IFNG gene that encodes interferon with ten amino-acid deletions at the C-terminal. We also generated genetic constructs that ensured the expression of native and modified bovine IFNG fused with GFP gene in yeast Pichia pastoris. The expression of IFN-γ/GFP and IFN-γ(Δ10)/GFP chimeric proteins showed that bovine IFN-γ nuclear localization signal was functioned in yeast cells. The absence of these proteins leads to the cytoplasmic accumulation of recombinant protein. {\textcopyright} 2010 Pleiades Publishing, Ltd.",
author = "A.E. Gradoboeva and M.V. Padkina",
year = "2010",
doi = "10.1134/S1990519X10060076",
language = "English",
volume = "4",
pages = "566--571",
journal = "Cell and Tissue Biology",
issn = "1990-519X",
publisher = "МАИК {"}Наука/Интерпериодика{"}",
number = "6",

}

RIS

TY - JOUR

T1 - Bovine gamma-interferon nuclear localization sequence provides translocation of recombinant protein to yeast Pichia pastoris cell nucleus

AU - Gradoboeva, A.E.

AU - Padkina, M.V.

PY - 2010

Y1 - 2010

N2 - It is known that the expression of heterologous protein production in microorganisms has a negative influence on the host cell. Therefore, to utilize microorganisms for production of recombinant proteins it is necessary the follow the fate of recombinant proteins in cells. In this study, we constructed a modified bovine IFNG gene that encodes interferon with ten amino-acid deletions at the C-terminal. We also generated genetic constructs that ensured the expression of native and modified bovine IFNG fused with GFP gene in yeast Pichia pastoris. The expression of IFN-γ/GFP and IFN-γ(Δ10)/GFP chimeric proteins showed that bovine IFN-γ nuclear localization signal was functioned in yeast cells. The absence of these proteins leads to the cytoplasmic accumulation of recombinant protein. © 2010 Pleiades Publishing, Ltd.

AB - It is known that the expression of heterologous protein production in microorganisms has a negative influence on the host cell. Therefore, to utilize microorganisms for production of recombinant proteins it is necessary the follow the fate of recombinant proteins in cells. In this study, we constructed a modified bovine IFNG gene that encodes interferon with ten amino-acid deletions at the C-terminal. We also generated genetic constructs that ensured the expression of native and modified bovine IFNG fused with GFP gene in yeast Pichia pastoris. The expression of IFN-γ/GFP and IFN-γ(Δ10)/GFP chimeric proteins showed that bovine IFN-γ nuclear localization signal was functioned in yeast cells. The absence of these proteins leads to the cytoplasmic accumulation of recombinant protein. © 2010 Pleiades Publishing, Ltd.

U2 - 10.1134/S1990519X10060076

DO - 10.1134/S1990519X10060076

M3 - Article

VL - 4

SP - 566

EP - 571

JO - Cell and Tissue Biology

JF - Cell and Tissue Biology

SN - 1990-519X

IS - 6

ER -

ID: 8183003