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Birgit Agne
Researcher at Martin Luther University of Halle-Wittenberg
Publications - 27
Citations - 1399
Birgit Agne is an academic researcher from Martin Luther University of Halle-Wittenberg. The author has contributed to research in topics: Translocon & Chloroplast. The author has an hindex of 15, co-authored 27 publications receiving 1238 citations. Previous affiliations of Birgit Agne include Ruhr University Bochum & University of Neuchâtel.
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Journal ArticleDOI
Pheophytin Pheophorbide Hydrolase (Pheophytinase) Is Involved in Chlorophyll Breakdown during Leaf Senescence in Arabidopsis
Silvia Schelbert,Sylvain Aubry,Bo Burla,Bo Burla,Birgit Agne,Felix Kessler,Karin Krupinska,Stefan Hörtensteiner +7 more
TL;DR: Pheophytinase (PPH), a chloroplast-located and senescence-induced hydrolase widely distributed in algae and land plants, is identified and proposed that the sequence of early chlorophyll catabolic reactions be revised.
Journal ArticleDOI
Pex8p: an intraperoxisomal organizer of the peroxisomal import machinery.
Birgit Agne,Nadja M Meindl,Karsten Niederhoff,Henrik Einwächter,Peter Rehling,Albert Sickmann,Helmut E. Meyer,Wolfgang Girzalsky,Wolf H. Kunau +8 more
TL;DR: It is concluded that Pex8p organizes the formation of the larger import complex from the trans side of the peroxisomal membrane and thus might enable functional communication between both sides of the membrane.
Journal ArticleDOI
The TOC complex: preprotein gateway to the chloroplast.
TL;DR: The current state of knowledge regarding the composition and function of the TOC complex is described, which consists of three types of components belonging to a small family: Toc34, Toc75 and Toc159.
Journal ArticleDOI
A toc159 import receptor mutant, defective in hydrolysis of GTP, supports preprotein import into chloroplasts.
Birgit Agne,Sibylle Infanger,Fei Wang,Valère Hofstetter,Gwendoline Rahim,Meryll Martin,Dong-Wook Lee,Inhwan Hwang,Danny J. Schnell,Felix Kessler +9 more
TL;DR: It is shown that atToc159 K868R can support protein import into isolated chloroplasts, albeit at lower preprotein binding and import efficiencies compared with the wild-type receptor, and it is concluded that GTP hydrolysis at atTOC159 is not strictly required for preprotein translocation.
Journal ArticleDOI
The Acidic A-Domain of Arabidopsis Toc159 Occurs as a Hyperphosphorylated Protein
Birgit Agne,Charles Andrès,Cyril Montandon,Bastien Christ,Anouk Ertan,Friederike Jung,Sibylle Infanger,Sylvain Bischof,Sacha Baginsky,Felix Kessler +9 more
TL;DR: In Arabidopsis, the A-domain is not simply degraded but that it accumulates as a soluble, phosphorylated protein separated from Toc159, which is a casein kinase 2-like activity.