{Reference Type}: Journal Article
{Title}: Insights into the tolerant function of VWA proteins in terms of expression analysis and RGLG5-VWA crystal structure.
{Author}: Wang Q;Tian S;Zhang X;Zhang Y;Wang Y;Xie S;
{Journal}: Plant Physiol Biochem
{Volume}: 214
{Issue}: 0
{Year}: 2024 Jun 21
{Factor}: 5.437
{DOI}: 10.1016/j.plaphy.2024.108864
{Abstract}: The VWA domain commonly functions as a crucial component of multiprotein complexes, facilitating protein-protein interactions. However, limited studies have focused on the systemic study of VWA proteins in plants. Here, we identified 28 VWA protein genes in Arabidopsis thaliana, categorized into three clades, with one tandem duplication event and four paralogous genes within collinearity blocks. Then, we determined their expression patterns under abiotic stresses by transcriptomic analysis. All five RGLG genes were found to be responsive to at least one kind of abiotic stress, and RGLG5 was identified as a multiple stress-responsive gene, coding an E3 ubiquitin ligase with a VWA domain and a C-terminal RING domain. Subsequently, we explored tolerant function of RGLG5 by determining the crystal structure of its VWA domain. The structural comparison revealed the allosteric regulation mechanism of RGLG5-VWA, wherein the deflection of α7 led to displacement of key residue binding metal ion within MIDAS motif. Our findings provide full-scale knowledge on VWA proteins, and insights into tolerant function of RGLG5-VWA in terms of crystal structure.