TY  - GEN
A1  - Sas, Claudia
A1  - Müller, Frank
A1  - Kappel, Christian
A1  - Kent, Tyler V.
A1  - Wright, Stephen I.
A1  - Hilker, Monika
A1  - Lenhard, Michael
T1  - Repeated inactivation of the first committed enzyme underlies the loss of benzaldehyde emission after the selfing transition in Capsella
T2  - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
N2  - The enormous species richness of flowering plants is at least partly due to floral diversification driven by interactions between plants and their animal pollinators [1, 2]. Specific pollinator attraction relies on visual and olfactory floral cues [3-5]; floral scent can not only attract pollinators but also attract or repel herbivorous insects [6-8]. However, despite its central role for plant-animal interactions, the genetic control of floral scent production and its evolutionary modification remain incompletely understood [9-13]. Benzenoids are an important class of floral scent compounds that are generated from phenylalanine via several enzymatic pathways [14-17]. Here we address the genetic basis of the loss of floral scent associated with the transition from outbreeding to selfing in the genus Capsella. While the outbreeding C. grandiflora emits benzaldehyde as a major constituent of its floral scent, this has been lost in the selfing C. rubella. We identify the Capsella CNL1 gene encoding cinnamate: CoA ligase as responsible for this variation. Population genetic analysis indicates that CNL1 has been inactivated twice independently in C. rubella via different novel mutations to its coding sequence. Together with a recent study in Petunia [18], this identifies cinnamate: CoA ligase as an evolutionary hotspot for mutations causing the loss of benzenoid scent compounds in association with a shift in the reproductive strategy of Capsella from pollination by insects to self-fertilization.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 904 
KW  - benzyl alcohol-dehydrogenase
KW  - floral scent
KW  - recent speciation
KW  - petunia flowers
KW  - genus capsella
KW  - evolution
KW  - biosynthesis
KW  - fragrance
KW  - purification
KW  - pollinators
KW  - benzaldehyde
KW  - selfing syndrome
KW  - shepherd’s purse
KW  - cinnamate:CoA ligase
Y1  - 2020
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-438018
SN  - 1866-8372
IS  - 904
SP  - 3313
EP  - 3319
ER  - 
TY  - GEN
A1  - Yan, Robert
A1  - Friemel, Martin
A1  - Aloisi, Claudia
A1  - Huynen, Martijn
A1  - Taylor, Ian A.
A1  - Leimkühler, Silke
A1  - Pastore, Annalisa
T1  - The eukaryotic-specific Isd11 is a complex- orphan protein with ability to bind the prokaryotic IscS
T2  - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
N2  - The eukaryotic protein Isd11 is a chaperone that binds and stabilizes the central component of the essential metabolic pathway responsible for formation of iron-sulfur clusters in mitochondria, the desulfurase Nfs1. Little is known about the exact role of Isd11. Here, we show that human Isd11 (ISD11) is a helical protein which exists in solution as an equilibrium between monomer, dimeric and tetrameric species when in the absence of human Nfs1 (NFS1). We also show that, surprisingly, recombinant ISD11 expressed in E. coli co-purifies with the bacterial orthologue of NFS1, IscS. Binding is weak but specific suggesting that, despite the absence of Isd11 sequences in bacteria, there is enough conservation between the two desulfurases to retain a similar mode of interaction. This knowledge may inform us on the conservation of the mode of binding of Isd11 to the desulfurase. We used evolutionary evidence to suggest Isd11 residues involved in the interaction.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 551 
KW  - sulfur cluster formation
KW  - Escherichia coli
KW  - cysteine desulfurase
KW  - interacting protein
KW  - bacterial frataxin
KW  - statistical-model
KW  - biogenesis
KW  - biosynthesis
KW  - NFS1
KW  - deficiency
Y1  - 2019
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-411906
SN  - 1866-8372
IS  - 551
ER  -