Fig. 5: Protein stability connectivity map of LSm and Sm proteins. | Nature Communications

Fig. 5: Protein stability connectivity map of LSm and Sm proteins.

From: Altered assembly paths mitigate interference among paralogous complexes

Fig. 5

A Schematic depiction of the subunit arrangement of the LSm- and Sm-type complexes. Paralogous proteins are represented by the same colors. The paralogous relationships between LSm and Sm proteins are indicated at right. B The protein stability-based interaction map of LSm/Sm proteins. The matrix heatmap represents log2-fold-change in protein stability of the protein indicated at left upon overproducing the protein indicated on top. LSm/Sm subunits are ordered according to the complex they are associated with and the subunit arrangement in the corresponding complex shown in (A). C A network diagram depicting the entire LSm/Sm protein stability-based interaction network, in which nodes are subunits and edges are interactions between two partners. Paralogous proteins are shown in the same colors. Positive/stabilization or negative/destabilization interactions are indicated as red or blue arrows, respectively. X→Y indicates that supplying X stabilizes/degrades Y, whereas X↔Y denotes that X and Y are mutually stabilizing/degrading. The thickness of the arrow lines is weighted according to the degree of interaction. D Protein stability analysis of LSm3 and LSm10 by GPS assays. E Protein stability analysis of proteins indicated on top with or without providing pICln. F Protein stability analysis of pICln with or without co-expressing the LSm/Sm proteins indicated at right. Source data are provided as a source data file.

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