
Choline transporter‐like1 (CHER1) is crucial for plasmodesmata ...
Map‐based cloning of one mutant revealed a point mutation in the choline transporter‐like 1 (CHER1) protein, changing glycine 247 into glutamate. Mutation in CHER1 resulted in a starch excess phenotype and stunted growth.
CHOLINE TRANSPORTER-LIKE1 is required for sieve plate ... - PubMed
Jul 10, 2014 · CHER1 encodes a member of a poorly characterized choline transporter-like protein family in plants and animals. We show that CHER1 facilitates choline transport, localizes to the trans-Golgi network, and during cytokinesis is associated with the phragmoplast.
CHOLINE TRANSPORTER-LIKE1 is required for sieve plate ... - Nature
Jul 10, 2014 · CHER1 encodes a member of a poorly characterized choline transporter-like protein family in plants and animals. We show that CHER1 facilitates choline transport, localizes to the...
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High Specificity in CheR Methyltransferase Function
Background: Many bacteria possess multiple CheR methyltransferases that methylate the conserved chemoreceptor signaling domains. Results: CheR2 of Pseudomonas putida is essential for chemotaxis, whereas CheR1 is required for efficient biofilm ...
CHER1 expression result in highly reduced PD number and the absence of complex PD in fully developed leaves, explaining reduced MP17–GFP fluorescence in mutant
Comparative proteomic profiling of the choline transporter‐like1 (CHER1 …
Leaves of cher1 mutant plants have up to 10 times less PD, which do not develop to complex structures. Here we utilize the T-DNA insertion mutant cher1–4 and report a deep comparative proteomic workflow for the identification of cell-wall-embedded PD-associated proteins.
Results: CheR2 of Pseudomonas putida is essential for chemotaxis, whereas CheR1 is required for efficient biofilm formation, and only CheR2 methylates chemotaxis receptors McpS and McpT. Conclusion: Paralogous CheR have different functions.
RCSB PDB - 5XLY: Crystal structure of CheR1 in complex with c-di …
May 12, 2017 · Recently, a single-domain PilZ protein, MapZ (PA4608), was identified to inhibit the activity of the methyltransferase CheR1. Here, crystal structures of the C-terminal domain of CheR1 containing SAH and of CheR1 in complex with c-di-GMP-bound MapZ are reported.
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