Arndt Wallmann's research while affiliated with University of Cambridge and other places
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Publications (13)
Determination of surface pKa values on PSII protein PsbO: Being close to the proton release side of Photosystem II and equipped with numerous surface carboxylate groups, PsbO is an appealing model to study side‐chain‐protonation reactions. Using solution NMR techniques, we were able to determine the pKa values of 21 out of 22 carboxylate groups, re...
Intrinsically disordered proteins and regions typically lack a well-defined structure and thus fall outside the scope of the classic sequence–structure–function relationship. Hence, classic sequence- or structure-based bioinformatic approaches are often not well suited to identify homology or predict the function of unknown intrinsically disordered...
Photosystem II (PSII) catalyzes the splitting of water, releasing protons and dioxygen. Its highly conserved subunit PsbO extends from the oxygen evolving center (OEC) into the thylakoid lumen and stabilizes the catalytic Mn 4 CaO 5 ‐cluster. The high conservation of accessible, negatively charged surface residues in PsbO suggests additional functi...
Microtubules are filamentous structures necessary for cell division, motility and morphology. Microtubule dynamics are critically regulated by microtubule-associated proteins (MAPs). We outline the molecular mechanism by which the MAP, COMPANION OF CELLULOSE SYNTHASE1 (CC1), controls microtubule-bundling and dynamics in plants under salt stress con...
Activation of the innate immune pattern recognition receptor NOD2 by the bacterial muramyl-dipeptide peptidoglycan fragment triggers recruitment of the downstream adaptor kinase RIP2, eventually leading to NF-κB activation and proinflammatory cytokine production. Here we show that full-length RIP2 can form long filaments mediated by its caspase rec...
Microtubules are filamentous structures necessary for cell division, motility and morphology, with dynamics critically regulated by microtubule-associated proteins (MAPs). We outline the molecular mechanism by which the MAP, COMPANION OF CELLULOSE SYNTHASE1 (CC1), controls microtubule bundling and dynamics to sustain plant growth under salt stress....
Citations
... This is an additional indication for a slight expansion of dPSIIcc in buffer solution. Since the latter expansion concerns largely the membrane-extrinsic parts of PSII, it may also be caused by a larger conformational flexibility in this region of dPSIIcc 254,292,293 . Fig. 1 ...
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... addition to the aforementioned DNA-free gene editing, DCIP could engender the delivery of nanobodies for pathogen resistance and targeted protein degradation 74,75 , the delivery of stress tolerance conferring disordered proteins 76 , or the delivery of a greater variety of morphogenic regulators to control plant regeneration. ...
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... 5,9). Such an extended water-mediated H-bond cluster of His and carboxylic sidechains is reminiscent of the proton-binding antennas thought to prolong the dwell time of the proton at the surface of proton-binding proteins [116][117][118][119][120][121][122]. In GPR68 with standard protonation states, His and carboxylic sidechains of the extracellular cluster inter-connect to the internal carboxylic triad via long-distance water-mediated H-bond paths (Figs. ...
... CSCs move along the plasma membrane at a speed of 200-350nm/min to synthesise cellulose, and their movement is thought to be driven by the catalytic activity of the CESAs (5). Various developmental and environmental factors regulate CSC activity to alter tissue growth (6). For example, CSC activity can be regulated through the phosphorylation of CESAs in response to light and hormonal signalling (7). ...
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... RIPK2 is an adaptor protein, which comprises a kinase and a caspase activation and recruitment domain (CARD) connected by a disordered intermediate loop (Humphries et al, 2015). RIPK2 recruitment to activated NOD receptor via CARD-CARD interactions, triggers RIPK2 autophosphorylation, filament formation (Pellegrini et al, 2018), and both Lys63-Ub and Met1-Ub ubiquitination. Ubiquitination is mediated by different E3 ligases including inhibitors of apoptosis (IAPs) and the linear ubiquitin chain complex (LUBAC) (Chin et al, 2002;Hasegawa et al, 2008;Bertrand et al, 2009;Tao et al, 2009;Damgaard et al, 2012;Boyle et al, 2014;Goncharov et al, 2018;Heim et al, 2020). ...
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