Antje Hellmuth
Leibniz Association
8 Papers
57 Citations
Antje Hellmuth is an academic researcher from Leibniz Association. The author has contributed to research in topics: Degron & Lateral root. The author has an hindex of 6, co-authored 8 publications. Previous affiliations of Antje Hellmuth include University of Washington.
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Papers
Auxin-induced degradation dynamics set the pace for lateral root development.
Jessica M. Guseman,Antje Hellmuth,Amy Lanctot,Tamar P. Feldman,Britney L. Moss,Eric Klavins,Luz Irina A. Calderón Villalobos,Jennifer L. Nemhauser +7 more
TL;DR: Progression through the well-established stages of lateral root development was strongly correlated with the engineered rates of IAA14 turnover, leading to the conclusion that Aux/IAAs are auxin-initiated timers that synchronize developmental transitions.
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Variation in auxin sensing guides AUX/IAA transcriptional repressor ubiquitylation and destruction
Martin Winkler,Michael Niemeyer,Antje Hellmuth,Philipp Janitza,Gideon Christ,Sophia L. Samodelov,Sophia L. Samodelov,Verona Wilde,Petra Majovsky,Marco Trujillo,Matias D. Zurbriggen,Wolfgang Hoehenwarter,Marcel Quint,Luz Irina A. Calderón Villalobos +13 more
TL;DR: It is postulated that the intrinsic flexibility of AUX/IAAs might bias their ubiquitylation and destruction kinetics enabling specific auxin responses, and evidence is presented for an evolving AUx/IAA repertoire, typified by the IAA6/ IAA19 ohnologues, that discriminates the range of auxin concentrations found in plants.
Rate Motifs Tune Auxin/Indole-3-Acetic Acid Degradation Dynamics
Britney L. Moss,Haibin Mao,Jessica M. Guseman,Thomas R. Hinds,Antje Hellmuth,Marlies Kovenock,Anisa Noorassa,Amy Lanctot,Luz Irina A. Calderón Villalobos,Ning Zheng,Jennifer L. Nemhauser +10 more
TL;DR: It is found that rate motifs can act by enhancing interaction between repressors and the E3, but that this is not the only mechanism of action.
Solution structure of the PsIAA4 oligomerization domain reveals interaction modes for transcription factors in early auxin response
Dhurvas Chandrasekaran Dinesh,Michael Kovermann,Mohanraj Gopalswamy,Antje Hellmuth,Luz Irina A. Calderón Villalobos,Hauke Lilie,Jochen Balbach,Steffen Abel,Steffen Abel,Steffen Abel +9 more
TL;DR: This work reports the solution structure of a wild-type AUX/IAA PB1 domain and identifies amino acid residues that engage in directional interaction of monomers, largely via hydrogen bonds between conserved basic and acidic surface patches, and provides a framework for unraveling molecular determinants that confer specificity to complex interactions between AUX-IAA and ARF transcription factors.
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Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies.
Michael Niemeyer,Elena Moreno Castillo,Christian Ihling,Claudio Iacobucci,Verona Wilde,Antje Hellmuth,Wolfgang Hoehenwarter,Sophia L. Samodelov,Matias D. Zurbriggen,Panagiotis L. Kastritis,Andrea Sinz,Luz Irina A. Calderón Villalobos +11 more
TL;DR: The authors show that intrinsically disordered regions near the degrons of two Aux/IAA proteins reinforce complex assembly and position AUX/IAAs for ubiquitylation, and establish a role for IDRs in modulating auxin receptor assemblies.