Genetic transformation of Arabidopsis lyrata: specific expression of the green fluorescent protein (GFP) in pistil tissues

2007 ◽  
Vol 26 (6) ◽  
pp. 745-753 ◽  
Author(s):  
Isabelle Fobis-Loisy ◽  
Pierre Chambrier ◽  
Thierry Gaude
Keyword(s):  
Green Fluorescent Protein ◽  
Genetic Transformation ◽  
Fluorescent Protein ◽  
Specific Expression ◽  
Arabidopsis Lyrata ◽  
Green Fluorescent

High level Purkinje cell specific expression of green fluorescent protein in transgenic mice

2001 ◽  
Vol 115 (6) ◽  
pp. 455-464 ◽  
Author(s):  
Xulun Zhang ◽  
Stephan L. Baader ◽  
Feng Bian ◽  
Wolfgang Müller ◽  
John Oberdick
Keyword(s):  
Green Fluorescent Protein ◽  
Transgenic Mice ◽  
Purkinje Cell ◽  
Fluorescent Protein ◽  
Specific Expression ◽  
Green Fluorescent ◽  
High Level

scholarly journals Transgenic Pigs with Pancreas-specific Expression of Green Fluorescent Protein

2014 ◽  
Vol 60 (3) ◽  
pp. 230-237 ◽  
Author(s):  
Hitomi MATSUNARI ◽  
Toshihiro KOBAYASHI ◽  
Masahito WATANABE ◽  
Kazuhiro UMEYAMA ◽  
Kazuaki NAKANO ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Transgenic Pigs ◽  
Specific Expression ◽  
Green Fluorescent

scholarly journals Genetic transformation of Coniochaeta sp. 2T2.1, key fungal member of a lignocellulose-degrading microbial consortium

2019 ◽  
Vol 4 (1) ◽  
Author(s):  
Nancy N Nichols ◽  
Ronald E Hector ◽  
Sarah E Frazer
Keyword(s):  
Green Fluorescent Protein ◽  
Genetic Transformation ◽  
Pure Culture ◽  
Ecological Niche ◽  
Fluorescent Protein ◽  
Microbial Consortium ◽  
Transformed Cells ◽  
Antibiotic Selection ◽  
Green Fluorescent ◽  
Selection Of

Abstract Coniochaeta sp. strain 2T2.1 is a key member of a microbial consortium that degrades lignocellulosic biomass. Due to its ecological niche and ability to also grow in pure culture on wheat straw, protocols for transformation and antibiotic selection of the strain were established. Hygromycin was found to be a reliable selectable transformation marker, and the mammalian codon-optimized green fluorescent protein was expressed and used to visualize fluorescence in transformed cells of strain 2T2.1.

Intestine-specific expression of green fluorescent protein-tagged cathepsin B: proof-of-principle experiments

2008 ◽  
Vol 0 (ja) ◽  
pp. 080808064931026-30
Author(s):  
Kristina Mayer ◽  
Maria E. Iolyeva ◽  
Ulf Meyer-Grahle ◽  
Klaudia Brix
Keyword(s):  
Green Fluorescent Protein ◽  
Cathepsin B ◽  
Fluorescent Protein ◽  
Specific Expression ◽  
Green Fluorescent ◽  
Proof Of Principle

Transgenic peach plants (Prunus persica L.) produced by genetic transformation of embryo sections using the green fluorescent protein (GFP) as an in vivo marker

2005 ◽  
Vol 14 (4) ◽  
pp. 419-427 ◽  
Author(s):  
Rosa M. P�rez-Clemente ◽  
Amparo P�rez-Sanju�n ◽  
Lorenzo Garc�a-F�rriz ◽  
Jos�-P�o Beltr�n ◽  
Luis A. Ca�as
Keyword(s):  
Green Fluorescent Protein ◽  
Genetic Transformation ◽  
Prunus Persica ◽  
Fluorescent Protein ◽  
Embryo Sections ◽  
Green Fluorescent

Intestine-specific expression of green fluorescent protein-tagged cathepsin B: proof-of-principle experiments

2008 ◽  
Vol 389 (8) ◽  
Author(s):  
Kristina Mayer ◽  
Maria E. Iolyeva ◽  
Ulf Meyer-Grahle ◽  
Klaudia Brix
Keyword(s):  
Transcription Factor ◽  
Green Fluorescent Protein ◽  
Cathepsin B ◽  
Fluorescent Protein ◽  
Regulatory Elements ◽  
Egfp Expression ◽  
Reporter Protein ◽  
Specific Expression ◽  
Green Fluorescent ◽  
Proof Of Principle

Abstract We hypothesized that tissue-specific expression of cathepsin B-enhanced green fluorescent protein (CB-EGFP) can be driven by the A33-antigen promoter that contains positive cis-regulatory elements, including caudal-related homeobox (CDX) binding sites. The intestine-specific transcription factor Cdx1 is crucial for A33-antigen promoter activation and could thereby induce expression of CB-EGFP. This concept was tested by construction of the vector pA33-CathB-EGFP encoding CB-EGFP downstream of the A33-antigen promoter. Its Cdx1 dependence, as an indication of its intestine-specific expression, was tested in Cdx1-negative CHO-K1 cells. Cdx1 expression was achieved upon transfection with pCdx1-DsRed-Express and was indicated by red fluorescence of the simultaneously translated reporter protein. Immunolabeling with Cdx1-specific antibodies showed correct targeting of the transcription factor to its point of action in nuclei of transfected cells. Co-transfection experiments with plasmids pA33-CathB-EGFP and pCdx1-DsRed-Express confirmed the hypothesis that Cdx1 indeed activates CB-EGFP expression in a manner dependent on the A33-antigen promoter. Co-localization with compartment-specific markers and subcellular fractionation confirmed CB-EGFP trafficking along the expected route to endolysosomal compartments. Hence, the A33-antigen promoter represents a potent tool for induction of Cdx1-dependent CB-EGFP expression in vitro. Our proof-of-principle studies confirm the suitability of this approach in visualizing protease transport in Cdx1-positive tissues of the gastrointestinal tract.

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